positive regulation of cytoplasmic translation / RNA polymerase complex / transcription elongation-coupled chromatin remodeling / submerged biofilm formation / stringent response / cellular response to cell envelope stress / regulation of DNA-templated transcription initiation / bacterial-type flagellum assembly / bacterial-type RNA polymerase core enzyme binding / cytosolic DNA-directed RNA polymerase complex ...positive regulation of cytoplasmic translation / RNA polymerase complex / transcription elongation-coupled chromatin remodeling / submerged biofilm formation / stringent response / cellular response to cell envelope stress / regulation of DNA-templated transcription initiation / bacterial-type flagellum assembly / bacterial-type RNA polymerase core enzyme binding / cytosolic DNA-directed RNA polymerase complex / bacterial-type flagellum-dependent cell motility / transcriptional attenuation / endoribonuclease inhibitor activity / RNA-binding transcription regulator activity / nitrate assimilation / positive regulation of ribosome biogenesis / translational termination / negative regulation of cytoplasmic translation / DnaA-L2 complex / translation repressor activity / negative regulation of DNA-templated DNA replication initiation / DNA-directed RNA polymerase complex / mRNA regulatory element binding translation repressor activity / assembly of large subunit precursor of preribosome / ribosome assembly / transcription elongation factor complex / regulation of DNA-templated transcription elongation / cytosolic ribosome assembly / response to reactive oxygen species / transcription antitermination / DNA-templated transcription initiation / cell motility / regulation of cell growth / DNA-templated transcription termination / response to radiation / mRNA 5'-UTR binding / ribonucleoside binding / DNA-directed RNA polymerase / DNA-directed RNA polymerase activity / ribosome biogenesis / large ribosomal subunit / ribosome binding / transferase activity / response to heat / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / protein-containing complex assembly / small ribosomal subunit rRNA binding / ribosomal large subunit assembly / cytosolic small ribosomal subunit / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / intracellular iron ion homeostasis / cytoplasmic translation / tRNA binding / single-stranded RNA binding / protein dimerization activity / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / response to antibiotic / negative regulation of DNA-templated transcription / mRNA binding / DNA-templated transcription / magnesium ion binding / DNA binding / RNA binding / zinc ion binding / metal ion binding / membrane / cytosol / cytoplasm Similarity search - Function
: / Ribosomal protein S1 / Ribosomal protein S1-like / : / Transcription antitermination protein, NusG / Transcription antitermination protein, NusG, bacteria, conserved site / Transcription termination factor nusG signature. / NusG-like / Transcription termination factor nusG / NusG, N-terminal ...: / Ribosomal protein S1 / Ribosomal protein S1-like / : / Transcription antitermination protein, NusG / Transcription antitermination protein, NusG, bacteria, conserved site / Transcription termination factor nusG signature. / NusG-like / Transcription termination factor nusG / NusG, N-terminal / In Spt5p, this domain may confer affinity for Spt4p. It possesses a RNP-like fold. / NusG, N-terminal domain superfamily / Ribosomal protein L10, eubacterial, conserved site / Ribosomal protein L10 signature. / Ribosomal protein L10 / S1 domain profile. / DNA-directed RNA polymerase, omega subunit / DNA-directed RNA polymerase, subunit beta-prime, bacterial type / DNA-directed RNA polymerase, beta subunit, external 1 domain superfamily / DNA-directed RNA polymerase, beta subunit, external 1 domain / RNA polymerase beta subunit external 1 domain / RNA polymerase, alpha subunit, C-terminal / Bacterial RNA polymerase, alpha chain C terminal domain / DNA-directed RNA polymerase, alpha subunit / DNA-directed RNA polymerase beta subunit, bacterial-type / Ribosomal protein L11, bacterial-type / Ribosomal protein S21, conserved site / Ribosomal protein S21 signature. / Ribosomal protein L25, short-form / Ribosomal protein S14, bacterial/plastid / Ribosomal protein S1-like RNA-binding domain / S1 RNA binding domain / Ribosomal protein L31 type A / Ribosomal protein S21 superfamily / S1 domain / Ribosomal protein S21 / Ribosomal protein S16, conserved site / Ribosomal protein S16 signature. / Ribosomal protein L31 signature. / Ribosomal protein S21 / Ribosomal protein L31 / Ribosomal protein L31 superfamily / Ribosomal protein L31 / Ribosomal protein L11, conserved site / Ribosomal protein L11 signature. / Ribosomal protein L10-like domain superfamily / Ribosomal protein L10P / Ribosomal protein L10 / Ribosomal protein L16 signature 1. / Ribosomal protein L21, conserved site / Ribosomal protein L21 signature. / Ribosomal protein L16 signature 2. / Ribosomal protein L16, conserved site / Ribosomal protein L6, conserved site / Ribosomal protein L6 signature 1. / : / Ribosomal protein L9 signature. / Ribosomal protein L9, bacteria/chloroplast / Ribosomal protein L9, C-terminal / Ribosomal protein L9, C-terminal domain / Ribosomal protein L9, C-terminal domain superfamily / Ribosomal protein L11, N-terminal / Ribosomal protein L11, N-terminal domain / Ribosomal protein L11/L12 / Ribosomal protein L11, C-terminal / Ribosomal protein L11, C-terminal domain superfamily / Ribosomal protein L11/L12, N-terminal domain superfamily / Ribosomal protein L11/L12 / Ribosomal protein L11, RNA binding domain / Ribosomal protein L17 signature. / Ribosomal L25p family / Ribosomal protein L25 / Ribosomal protein L36 signature. / Ribosomal protein L32p, bacterial type / Ribosomal protein L28/L24 superfamily / Ribosomal protein L25/Gln-tRNA synthetase, N-terminal / Ribosomal protein L25/Gln-tRNA synthetase, anti-codon-binding domain superfamily / : / Ribosomal protein L9, N-terminal domain superfamily / Ribosomal protein L9 / Ribosomal protein L9, N-terminal / Ribosomal protein L9, N-terminal domain / Ribosomal protein L33, conserved site / Ribosomal protein L33 signature. / Ribosomal protein L35, conserved site / Ribosomal protein L35 signature. / Ribosomal protein L28 / Ribosomal protein L35, non-mitochondrial / Ribosomal protein L18, bacterial-type / : / Ribosomal protein L6, bacterial-type / Ribosomal protein S19, bacterial-type / Ribosomal protein S3, bacterial-type / Ribosomal protein S13, bacterial-type / Ribosomal protein S6, conserved site / Ribosomal protein S6 signature. / Ribosomal protein S7, bacterial/organellar-type / Ribosomal protein L9/RNase H1, N-terminal / DNA-directed RNA polymerase, subunit beta-prime / Ribosomal protein S11, bacterial-type Similarity search - Domain/homology
PHENYLALANINE / : / : / : / DNA / DNA (> 10) / RNA / RNA (> 10) / RNA (> 100) / RNA (> 1000) ...PHENYLALANINE / : / : / : / DNA / DNA (> 10) / RNA / RNA (> 10) / RNA (> 100) / RNA (> 1000) / 50S ribosomal protein L10 / Small ribosomal subunit protein uS5 / Large ribosomal subunit protein bL36 / Small ribosomal subunit protein bS18 / Small ribosomal subunit protein uS12 / Small ribosomal subunit protein uS10 / Small ribosomal subunit protein uS19 / Small ribosomal subunit protein uS3 / Small ribosomal subunit protein uS17 / Small ribosomal subunit protein uS14 / Small ribosomal subunit protein uS8 / Small ribosomal subunit protein uS13 / Small ribosomal subunit protein uS11 / Small ribosomal subunit protein uS4 / Small ribosomal subunit protein uS9 / Small ribosomal subunit protein uS15 / Small ribosomal subunit protein bS21 / Small ribosomal subunit protein bS16 / Small ribosomal subunit protein uS2 / Small ribosomal subunit protein bS20 / Small ribosomal subunit protein uS7 / Large ribosomal subunit protein uL15 / Large ribosomal subunit protein uL11 / Large ribosomal subunit protein bL19 / Large ribosomal subunit protein bL20 / Large ribosomal subunit protein bL27 / Large ribosomal subunit protein bL28 / Large ribosomal subunit protein uL29 / Large ribosomal subunit protein bL32 / Large ribosomal subunit protein bL33 / Large ribosomal subunit protein bL34 / Large ribosomal subunit protein bL35 / Large ribosomal subunit protein bL9 / DNA-directed RNA polymerase subunit alpha / DNA-directed RNA polymerase subunit omega / DNA-directed RNA polymerase subunit beta' / DNA-directed RNA polymerase subunit beta / Large ribosomal subunit protein uL13 / Large ribosomal subunit protein uL14 / Large ribosomal subunit protein uL16 / Large ribosomal subunit protein uL23 / Transcription termination/antitermination protein NusG / Large ribosomal subunit protein bL17 / Large ribosomal subunit protein bL21 / Large ribosomal subunit protein uL30 / Large ribosomal subunit protein uL6 / Small ribosomal subunit protein bS1 / Large ribosomal subunit protein uL18 / Large ribosomal subunit protein uL2 / Large ribosomal subunit protein uL3 / Large ribosomal subunit protein uL24 / Large ribosomal subunit protein uL4 / Large ribosomal subunit protein uL22 / Large ribosomal subunit protein uL5 / Large ribosomal subunit protein bL25 / Large ribosomal subunit protein bL31 / Small ribosomal subunit protein bS6 Similarity search - Component
Biological species
Escherichia coli (E. coli) synthetic construct (others)
Method
ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.4 Å
French Infrastructure for Integrated Structural Biology (FRISBI)
ANR-10-INBS-05
France
French National Research Agency
ANR-10-LABX-0030-INRT
France
French National Research Agency
ANR-10-IDEX-0002-02
France
European Molecular Biology Organization (EMBO)
LTF375-2019
France
Citation
Journal: Science / Year: 2020 Title: Structural basis of transcription-translation coupling and collision in bacteria. Authors: Michael William Webster / Maria Takacs / Chengjin Zhu / Vita Vidmar / Ayesha Eduljee / Mo'men Abdelkareem / Albert Weixlbaumer / Abstract: Prokaryotic messenger RNAs (mRNAs) are translated as they are transcribed. The lead ribosome potentially contacts RNA polymerase (RNAP) and forms a supramolecular complex known as the expressome. The ...Prokaryotic messenger RNAs (mRNAs) are translated as they are transcribed. The lead ribosome potentially contacts RNA polymerase (RNAP) and forms a supramolecular complex known as the expressome. The basis of expressome assembly and its consequences for transcription and translation are poorly understood. Here, we present a series of structures representing uncoupled, coupled, and collided expressome states determined by cryo-electron microscopy. A bridge between the ribosome and RNAP can be formed by the transcription factor NusG, which stabilizes an otherwise-variable interaction interface. Shortening of the intervening mRNA causes a substantial rearrangement that aligns the ribosome entrance channel to the RNAP exit channel. In this collided complex, NusG linkage is no longer possible. These structures reveal mechanisms of coordination between transcription and translation and provide a framework for future study.
History
Deposition
Jul 20, 2020
Deposition site: PDBE / Processing site: PDBE
Revision 1.0
Sep 16, 2020
Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 1 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 2 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 3 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 4 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 5 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 6 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 7 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 8 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 9 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 10 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 11 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 12 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 13 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 14 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 15 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 16 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: FSC / Data content type: FSC / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 1 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 2 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 3 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 4 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 5 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 6 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 7 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 8 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 9 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 10 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 11 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 12 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 13 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 14 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 15 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 16 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: FSC / Data content type: FSC / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 1 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 2 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 3 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 4 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 5 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 6 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 7 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 8 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 9 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 10 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 11 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 12 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 13 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 14 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 15 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Additional map / Part number: 16 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: FSC / Data content type: FSC / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0
Sep 16, 2020
Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release
Data content type: EM metadata / Data content type: EM metadata / Group: Experimental summary / Data content type: EM metadata / Category: em_admin / Data content type: EM metadata / Item: _em_admin.last_update
Mass: 499888.406 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: GenBank: CP054232.1
#22: RNA chain
mRNA
Mass: 17060.258 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)
#23: RNA chain
tRNA(fmet) P-site
Mass: 24832.918 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Production host: Escherichia coli (E. coli)
#24: RNA chain
Phe-NH-tRNA(Phe) A-site
Mass: 24751.018 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Production host: Escherichia coli (E. coli) / References: GenBank: CP054236.1
#26: RNA chain
23SribosomalRNA
Mass: 941820.562 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli)
#27: RNA chain
5SribosomalRNA
Mass: 38790.090 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: GenBank: CP035706.1
+
30S ribosomal protein ... , 21 types, 21 molecules ABACADAEAFAGAHAIAJAKALAMANAOAPAQARASATAUAY
#2: Protein
30SribosomalproteinS2
Mass: 26781.670 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: C3TPN2
#3: Protein
30SribosomalproteinS3
Mass: 26031.316 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: C3SQX2
#4: Protein
30SribosomalproteinS4
Mass: 23514.199 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: C3SR62
#5: Protein
30SribosomalproteinS5
Mass: 17617.455 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: A0A090BZW5
#6: Protein
30SribosomalproteinS6
Mass: 15197.032 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: W8T6F0
#7: Protein
30SribosomalproteinS7 / Small ribosomal subunit protein uS7
Mass: 17637.445 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P02359
#8: Protein
30SribosomalproteinS8
Mass: 14146.557 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: C3SR12
#9: Protein
30SribosomalproteinS9
Mass: 14886.270 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: C3SRY2
#10: Protein
30SribosomalproteinS10
Mass: 11755.597 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: C3SQT7
#11: Protein
30SribosomalproteinS11
Mass: 13870.975 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: C3SR57
#12: Protein
30SribosomalproteinS12
Mass: 13814.249 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: C3SQR7
#13: Protein
30SribosomalproteinS13
Mass: 13128.467 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: C3SR52
#14: Protein
30SribosomalproteinS14
Mass: 11606.560 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: C3SR07
#15: Protein
30SribosomalproteinS15
Mass: 10290.816 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: C3SSQ7
#16: Protein
30SribosomalproteinS16
Mass: 9207.572 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: C3SYP2
#17: Protein
30SribosomalproteinS17
Mass: 9724.491 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: C3SQY7
#18: Protein
30SribosomalproteinS18
Mass: 9005.472 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: C3SFP7
#19: Protein
30SribosomalproteinS19
Mass: 10455.355 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: C3SQW2
#20: Protein
30SribosomalproteinS20
Mass: 9708.464 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: C3TRH7
#21: Protein
30SribosomalproteinS21
Mass: 8524.039 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: C3STZ7
#25: Protein
30SribosomalproteinS1 / Bacteriophage Q beta RNA-directed RNA polymerase subunit I / Small ribosomal subunit protein bS1
Mass: 61238.887 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P0AG67
+
50S ribosomal protein ... , 31 types, 31 molecules BCBDBEBFBGBHBIBJBKBLBMBNBOBPBQBRBSBTBUBVBWBXBYBZB1B2B3B4B5B6B7
#28: Protein
50SribosomalproteinL2 / ribosomal protein uL2
Mass: 29923.619 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P60422
#29: Protein
50SribosomalproteinL3 / Large ribosomal subunit protein uL3
Mass: 22291.562 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P60438
#30: Protein
50SribosomalproteinL4 / ribosomal protein uL4
Mass: 22121.566 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P60723
#31: Protein
50SribosomalproteinL5 / ribosomal protein uL5
Mass: 20333.611 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P62399
#32: Protein
50SribosomalproteinL6 / ribosomal protein uL6
Mass: 18932.791 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P0AG55
#33: Protein
50SribosomalproteinL9 / ribosomal protein bL9
Mass: 15789.020 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P0A7R1
#34: Protein
50SribosomalproteinL10
Mass: 17736.596 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: A0A073UC57
#35: Protein
50SribosomalproteinL11 / ribosomal protein uL11
Mass: 14894.362 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P0A7J7
#36: Protein
50SribosomalproteinL13 / ribosomal protein uL13
Mass: 16050.606 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P0AA10
#37: Protein
50SribosomalproteinL14 / ribosomal protein uL14
Mass: 13565.067 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P0ADY3
#38: Protein
50SribosomalproteinL15 / Large ribosomal subunit protein uL15
Mass: 14994.443 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P02413
#39: Protein
50SribosomalproteinL16 / Large ribosomal subunit protein uL16
Mass: 15327.261 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P0ADY7
#40: Protein
50SribosomalproteinL17 / ribosomal protein bL17
Mass: 14393.657 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P0AG44
#41: Protein
50SribosomalproteinL18 / ribosomal protein uL18
Mass: 12794.668 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P0C018
#42: Protein
50SribosomalproteinL19 / ribosomal protein bL19
Mass: 13159.278 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P0A7K6
#43: Protein
50SribosomalproteinL20 / ribosomal protein bL20
Mass: 13528.024 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P0A7L3
#44: Protein
50SribosomalproteinL21 / ribosomal protein bL21
Mass: 11586.374 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P0AG48
#45: Protein
50SribosomalproteinL22 / ribosomal protein uL22
Mass: 12253.359 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P61175
#46: Protein
50SribosomalproteinL23 / ribosomal protein uL23
Mass: 11222.160 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P0ADZ0
#47: Protein
50SribosomalproteinL24 / ribosomal protein uL24
Mass: 11339.250 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P60624
#48: Protein
50SribosomalproteinL25 / ribosomal protein bL25
Mass: 10713.465 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P68919
#49: Protein
50SribosomalproteinL27 / ribosomal protein bL27
Mass: 9146.540 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P0A7L8
#50: Protein
50SribosomalproteinL28 / ribosomal protein bL28
Mass: 9027.551 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P0A7M2
#51: Protein
50SribosomalproteinL29 / ribosomal protein uL29
Mass: 7286.464 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P0A7M6
#52: Protein
50SribosomalproteinL30 / ribosomal protein uL30
Mass: 6554.820 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P0AG51
#53: Protein
50SribosomalproteinL32 / ribosomal protein bL32
Mass: 6463.445 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P0A7N4
#54: Protein
50SribosomalproteinL33 / ribosomal protein bL33
Mass: 6388.631 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P0A7N9
#55: Protein/peptide
50SribosomalproteinL34 / ribosomal protein bL34
Mass: 5397.463 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P0A7P5
#56: Protein
50SribosomalproteinL35 / Ribosomal protein A / ribosomal protein bL35
Mass: 7313.032 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P0A7Q1
#57: Protein/peptide
50SribosomalproteinL36
Mass: 5720.060 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: A0A2X1PTA3
#58: Protein
50SribosomalproteinL31
Mass: 7887.117 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: U9XX47
-
DNA chain , 2 types, 2 molecules CNCT
#59: DNA chain
Non-templateDNAstrand
Mass: 12063.754 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)
#60: DNA chain
TemplateDNAstrand
Mass: 11872.596 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)
In the structure databanks used in Yorodumi, some data are registered as the other names, "COVID-19 virus" and "2019-nCoV". Here are the details of the virus and the list of structure data.
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)
EMDB accession codes are about to change! (news from PDBe EMDB page)
The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
The EM Navigator/Yorodumi systems omit the EMD- prefix.
Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator
Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.
Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi