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Yorodumi- PDB-4woi: 4,5-linked aminoglycoside antibiotics regulate the bacterial ribo... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4woi | ||||||||||||||||||||||||
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Title | 4,5-linked aminoglycoside antibiotics regulate the bacterial ribosome by targeting dynamic conformational processes within intersubunit bridge B2 | ||||||||||||||||||||||||
Components |
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Keywords | RIBOSOME / Protein biosynthesis / ribosomes / paromomycin / antibiotic translocation / RNA / tRNA / transfer / exit / peptidyl / 30S / 70S / 16S / ribosomal subunit | ||||||||||||||||||||||||
Function / homology | Function and homology information cytoplasmic translational termination / stringent response / ribosomal large subunit binding / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / misfolded RNA binding / Group I intron splicing / RNA folding / transcriptional attenuation / endoribonuclease inhibitor activity ...cytoplasmic translational termination / stringent response / ribosomal large subunit binding / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / misfolded RNA binding / Group I intron splicing / RNA folding / transcriptional attenuation / endoribonuclease inhibitor activity / RNA-binding transcription regulator activity / positive regulation of ribosome biogenesis / negative regulation of cytoplasmic translation / four-way junction DNA binding / translational termination / DnaA-L2 complex / translation repressor activity / negative regulation of DNA-templated DNA replication initiation / negative regulation of translational initiation / regulation of mRNA stability / mRNA regulatory element binding translation repressor activity / ribosome assembly / assembly of large subunit precursor of preribosome / positive regulation of RNA splicing / transcription elongation factor complex / cytosolic ribosome assembly / regulation of DNA-templated transcription elongation / DNA endonuclease activity / response to reactive oxygen species / transcription antitermination / regulation of cell growth / DNA-templated transcription termination / maintenance of translational fidelity / response to radiation / mRNA 5'-UTR binding / ribosomal small subunit biogenesis / small ribosomal subunit rRNA binding / large ribosomal subunit / ribosome biogenesis / ribosome binding / regulation of translation / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / large ribosomal subunit rRNA binding / transferase activity / cytosolic small ribosomal subunit / ribosomal large subunit assembly / cytoplasmic translation / cytosolic large ribosomal subunit / tRNA binding / molecular adaptor activity / negative regulation of translation / rRNA binding / ribosome / structural constituent of ribosome / translation / response to antibiotic / negative regulation of DNA-templated transcription / mRNA binding / DNA binding / RNA binding / zinc ion binding / membrane / cytosol / cytoplasm Similarity search - Function | ||||||||||||||||||||||||
Biological species | Escherichia coli str. K-12 substr. MDS42 (bacteria) Escherichia coli (E. coli) Thermus thermophilus (bacteria) Enterobacteria phage L1 (virus) | ||||||||||||||||||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 3 Å | ||||||||||||||||||||||||
Model details | This structure consists of multiple PDB entries | ||||||||||||||||||||||||
Authors | Pulk, A. / Cate, J.H.D. / Blanchard, S. / Wasserman, M. / Altman, R. / Zhou, Z. / Zinder, J. / Green, K. / Garneau-Tsodikova, S. | ||||||||||||||||||||||||
Funding support | United States, 7items
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Citation | Journal: Nat Commun / Year: 2015 Title: Chemically related 4,5-linked aminoglycoside antibiotics drive subunit rotation in opposite directions. Authors: Wasserman, M.R. / Pulk, A. / Zhou, Z. / Altman, R.B. / Zinder, J.C. / Green, K.D. / Garneau-Tsodikova, S. / Doudna Cate, J.H. / Blanchard, S.C. | ||||||||||||||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4woi.cif.gz | 7.4 MB | Display | PDBx/mmCIF format |
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PDB format | pdb4woi.ent.gz | Display | PDB format | |
PDBx/mmJSON format | 4woi.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4woi_validation.pdf.gz | 7.5 MB | Display | wwPDB validaton report |
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Full document | 4woi_full_validation.pdf.gz | 8.2 MB | Display | |
Data in XML | 4woi_validation.xml.gz | 687.7 KB | Display | |
Data in CIF | 4woi_validation.cif.gz | 1014.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wo/4woi ftp://data.pdbj.org/pub/pdb/validation_reports/wo/4woi | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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2 |
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Unit cell |
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Details | There are 2 biological units in the assymetric unit. Each unit (ribosome) contains two subunits. |
-Components
-RNA chain , 5 types, 10 molecules AADAAWDVAXDWBACABBCB
#1: RNA chain | Mass: 499690.031 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) Escherichia coli str. K-12 substr. MDS42 (bacteria) References: GenBank: 359330873 #23: RNA chain | Mass: 5170.151 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) Enterobacteria phage L1 (virus) #24: RNA chain | Mass: 24485.539 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) Escherichia coli str. K-12 substr. MDS42 (bacteria) References: GenBank: 359330873 #25: RNA chain | Mass: 941612.375 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) Escherichia coli str. K-12 substr. MDS42 (bacteria) References: GenBank: 359330873 #26: RNA chain | Mass: 38790.090 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) Escherichia coli str. K-12 substr. MDS42 (bacteria) References: GenBank: 359330873 |
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-30S ribosomal protein ... , 20 types, 40 molecules ABDBACDCADDDAEDEAFDFAGDGAHDHAIDIAJDJAKDKALDLAMDMANDNAODOAPDP...
#2: Protein | Mass: 26781.670 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K12 / References: UniProt: P0A7V0 #3: Protein | Mass: 26031.316 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K12 / References: UniProt: P0A7V3 #4: Protein | Mass: 23514.199 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K12 / References: UniProt: P0A7V8 #5: Protein | Mass: 17629.398 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K12 / References: UniProt: P0A7W1 #6: Protein | Mass: 15727.512 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K12 / References: UniProt: P02358 #7: Protein | Mass: 20055.156 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K12 / References: UniProt: P02359 #8: Protein | Mass: 14146.557 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K12 / References: UniProt: P0A7W7 #9: Protein | Mass: 14886.270 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K12 / References: UniProt: P0A7X3 #10: Protein | Mass: 11755.597 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K12 / References: UniProt: P0A7R5 #11: Protein | Mass: 13870.975 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K12 / References: UniProt: P0A7R9 #12: Protein | Mass: 13768.157 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K12 / References: UniProt: P0A7S3 #13: Protein | Mass: 13128.467 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K12 / References: UniProt: P0A7S9 #14: Protein | Mass: 11606.560 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K12 / References: UniProt: P0AG59 #15: Protein | Mass: 10319.882 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: O157:H7 strain TW14359 / References: UniProt: C6UUI7 #16: Protein | Mass: 9207.572 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K12 / References: UniProt: P0A7T3 #17: Protein | Mass: 9724.491 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K12 / References: UniProt: P0AG63 #18: Protein | Mass: 9005.472 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K12 / References: UniProt: P0A7T7 #19: Protein | Mass: 10455.355 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K12 / References: UniProt: P0A7U3 #20: Protein | Mass: 9708.464 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K12 / References: UniProt: P0A7U7 #21: Protein | Mass: 8524.039 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K12 / References: UniProt: P68679 |
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-Protein , 1 types, 1 molecules AV
#22: Protein | Mass: 20671.621 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K12 / References: UniProt: P0A805 |
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+50S ribosomal protein ... , 30 types, 59 molecules BCCCBDCDBECEBFCFBGCGBHCHBICIBJCJBKCKBLCLBMCMBNCNBOCOBPCPBQCQ...
-Non-polymers , 4 types, 2237 molecules
#57: Chemical | ChemComp-MG / #58: Chemical | ChemComp-PAR / #59: Chemical | #60: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.2 Å3/Da / Density % sol: 61.8 % |
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Crystal grow | Temperature: 291 K / Method: microbatch / pH: 6.5 / Details: PEG8k, MPD, KCl, KSCN |
-Data collection
Diffraction |
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Diffraction source |
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Detector |
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Radiation |
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Radiation wavelength | Wavelength: 1.1 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 2.9→70 Å / Num. obs: 914752 / % possible obs: 73.7 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 73.274 Å2 / Rmerge F obs: 0.996 / Rmerge(I) obs: 0.163 / Rrim(I) all: 0.178 / Χ2: 1.029 / Net I/σ(I): 6.29 / Num. measured all: 4371132 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1 / Rejects: _
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-Phasing
Phasing | Method: molecular replacement |
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: IN-HOUSE STRUCTURE CONTAINING ALL RIBOSOMAL PROTEINS IN ONE CHAIN AND RRNA IN ANOTHER Resolution: 3→70 Å / Cross valid method: FREE R-VALUE
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Displacement parameters | Biso max: 538.28 Å2 / Biso mean: 101.9156 Å2 / Biso min: 3.31 Å2 | ||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3→70 Å
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