[English] 日本語
Yorodumi
- EMDB-9037: Mycobacterium tuberculosis RNAP open promoter complex with RbpA/C... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-9037
TitleMycobacterium tuberculosis RNAP open promoter complex with RbpA/CarD and AP3 promoter
Map data
Sample
  • Complex: Mycobacterium tuberculosis RNAP open promoter complex
    • Protein or peptide: x 7 types
    • DNA: x 2 types
  • Ligand: x 2 types
Keywordsinitiation / transcription bubble / closed clamp / open promoter complex / TRANSCRIPTION / TRANSCRIPTION-DNA complex
Function / homology
Function and homology information


bacterial-type RNA polymerase holo enzyme binding / response to water / Antimicrobial action and antimicrobial resistance in Mtb / bacterial-type RNA polymerase core enzyme binding / sigma factor activity / rRNA transcription / DNA-directed RNA polymerase complex / peptidoglycan-based cell wall / DNA-templated transcription initiation / ribonucleoside binding ...bacterial-type RNA polymerase holo enzyme binding / response to water / Antimicrobial action and antimicrobial resistance in Mtb / bacterial-type RNA polymerase core enzyme binding / sigma factor activity / rRNA transcription / DNA-directed RNA polymerase complex / peptidoglycan-based cell wall / DNA-templated transcription initiation / ribonucleoside binding / DNA-directed 5'-3' RNA polymerase activity / DNA-directed RNA polymerase / nucleic acid binding / protein dimerization activity / response to antibiotic / DNA-templated transcription / positive regulation of DNA-templated transcription / magnesium ion binding / DNA binding / zinc ion binding / plasma membrane / cytosol / cytoplasm
Similarity search - Function
CarD-like, C-terminal domain / : / : / CarD, C-terminal domain / RNA polymerase-binding protein RbpA / RbpA superfamily / RNA polymerase-binding protein / CarD-like/TRCF, RNAP-interacting domain / CarD-like/TRCF, RNAP-interacting domain superfamily / CarD-like/TRCF RID domain ...CarD-like, C-terminal domain / : / : / CarD, C-terminal domain / RNA polymerase-binding protein RbpA / RbpA superfamily / RNA polymerase-binding protein / CarD-like/TRCF, RNAP-interacting domain / CarD-like/TRCF, RNAP-interacting domain superfamily / CarD-like/TRCF RID domain / CarD-like/TRCF domain / Sigma-70 factors family signature 1. / RNA polymerase sigma factor RpoD, C-terminal / RNA polymerase sigma factor RpoD / : / RNA polymerase sigma-70 region 1.2 / Sigma-70 factor, region 1.2 / RNA polymerase sigma-70 region 3 / Sigma-70 region 3 / Sigma-70 factors family signature 2. / RNA polymerase sigma-70 / RNA polymerase sigma-70 region 4 / Sigma-70, region 4 / RNA polymerase sigma-70 region 2 / RNA polymerase sigma-70 like domain / Sigma-70 region 2 / RNA polymerase sigma factor, region 2 / RNA polymerase sigma factor, region 3/4-like / 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 / RNA polymerase Rpb6 / RNA polymerase, subunit omega/Rpo6/RPB6 / RNA polymerase Rpb6 / RNA polymerase Rpb1, domain 3 superfamily / RPB6/omega subunit-like superfamily / RNA polymerase Rpb1, clamp domain superfamily / RNA polymerase Rpb2, domain 2 superfamily / RNA polymerase Rpb1, domain 3 / RNA polymerase Rpb1, domain 3 / DNA-directed RNA polymerase, subunit beta-prime / RNA polymerase Rpb1, domain 1 / RNA polymerase Rpb1, domain 1 / DNA-directed RNA polymerase, insert domain / DNA-directed RNA polymerase, RpoA/D/Rpb3-type / RNA polymerase Rpb3/RpoA insert domain / RNA polymerase Rpb3/Rpb11 dimerisation domain / RNA polymerases D / RNA polymerase, alpha subunit / RNA polymerase Rpb1, domain 5 / RNA polymerase Rpb1, domain 4 / RNA polymerase Rpb1, domain 2 / RNA polymerase Rpb1, domain 5 / RNA polymerase Rpb1, domain 4 / RNA polymerase, beta subunit, protrusion / RNA polymerase beta subunit / RNA polymerase, N-terminal / RNA polymerase Rpb1, funnel domain superfamily / RNA polymerase I subunit A N-terminus / DNA-directed RNA polymerase, insert domain superfamily / RNA polymerase, RBP11-like subunit / RNA polymerase Rpb2, domain 2 / RNA polymerase Rpb2, domain 2 / RNA polymerase, beta subunit, conserved site / RNA polymerase Rpb2, domain 7 / RNA polymerase Rpb2, domain 3 / RNA polymerase Rpb2, OB-fold / RNA polymerase Rpb2, domain 7 / RNA polymerase Rpb2, domain 3 / RNA polymerases beta chain signature. / DNA-directed RNA polymerase, subunit 2, hybrid-binding domain / DNA-directed RNA polymerase, subunit 2 / DNA-directed RNA polymerase, subunit 2, hybrid-binding domain superfamily / RNA polymerase Rpb2, domain 6 / Winged helix-like DNA-binding domain superfamily
Similarity search - Domain/homology
DNA-directed RNA polymerase subunit omega / DNA-directed RNA polymerase subunit beta' / DNA-directed RNA polymerase subunit alpha / RNA polymerase sigma factor SigA / RNA polymerase sigma factor SigA / DNA-directed RNA polymerase subunit omega / DNA-directed RNA polymerase subunit beta' / DNA-directed RNA polymerase subunit beta / DNA-directed RNA polymerase subunit alpha / RNA polymerase-binding protein RbpA ...DNA-directed RNA polymerase subunit omega / DNA-directed RNA polymerase subunit beta' / DNA-directed RNA polymerase subunit alpha / RNA polymerase sigma factor SigA / RNA polymerase sigma factor SigA / DNA-directed RNA polymerase subunit omega / DNA-directed RNA polymerase subunit beta' / DNA-directed RNA polymerase subunit beta / DNA-directed RNA polymerase subunit alpha / RNA polymerase-binding protein RbpA / RNA polymerase-binding protein RbpA / RNA polymerase-binding transcription factor CarD / RNA polymerase-binding transcription factor CarD / DNA-directed RNA polymerase subunit beta
Similarity search - Component
Biological speciesMycobacterium tuberculosis (bacteria)
Methodsingle particle reconstruction / cryo EM
AuthorsDarst SA / Campbell EA
CitationJournal: Nature / Year: 2019
Title: Structures of an RNA polymerase promoter melting intermediate elucidate DNA unwinding.
Authors: Hande Boyaci / James Chen / Rolf Jansen / Seth A Darst / Elizabeth A Campbell /
Abstract: A key regulated step of transcription is promoter melting by RNA polymerase (RNAP) to form the open promoter complex. To generate the open complex, the conserved catalytic core of the RNAP combines ...A key regulated step of transcription is promoter melting by RNA polymerase (RNAP) to form the open promoter complex. To generate the open complex, the conserved catalytic core of the RNAP combines with initiation factors to locate promoter DNA, unwind 12-14 base pairs of the DNA duplex and load the template-strand DNA into the RNAP active site. Formation of the open complex is a multi-step process during which transient intermediates of unknown structure are formed. Here we present cryo-electron microscopy structures of bacterial RNAP-promoter DNA complexes, including structures of partially melted intermediates. The structures show that late steps of promoter melting occur within the RNAP cleft, delineate key roles for fork-loop 2 and switch 2-universal structural features of RNAP-in restricting access of DNA to the RNAP active site, and explain why clamp opening is required to allow entry of single-stranded template DNA into the active site. The key roles of fork-loop 2 and switch 2 suggest a common mechanism for late steps in promoter DNA opening to enable gene expression across all domains of life.
History
Header (metadata) releaseFeb 28, 2018-
DepositionAug 10, 2018-
Map releaseNov 21, 2018-
UpdateMar 13, 2024-
Current statusMar 13, 2024Processing site: RCSB / Status: Released

-
Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.3
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by radius
  • Surface level: 0.3
  • Imaged by UCSF Chimera
  • Download
  • Surface view with fitted model
  • Atomic models: PDB-6edt
  • Surface level: 0.3
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_9037.map.gz / Format: CCP4 / Size: 59.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.3 Å/pix.
x 250 pix.
= 325. Å
1.3 Å/pix.
x 250 pix.
= 325. Å
1.3 Å/pix.
x 250 pix.
= 325. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.3 Å
Density
Contour LevelBy AUTHOR: 0.25 / Movie #1: 0.3
Minimum - Maximum-0.7299977 - 1.9311254
Average (Standard dev.)0.006558573 (±0.07501595)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions250250250
Spacing250250250
CellA=B=C: 325.0 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.31.31.3
M x/y/z250250250
origin x/y/z0.0000.0000.000
length x/y/z325.000325.000325.000
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ240240240
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS250250250
D min/max/mean-0.7301.9310.007

-
Supplemental data

-
Sample components

+
Entire : Mycobacterium tuberculosis RNAP open promoter complex

EntireName: Mycobacterium tuberculosis RNAP open promoter complex
Components
  • Complex: Mycobacterium tuberculosis RNAP open promoter complex
    • Protein or peptide: DNA-directed RNA polymerase subunit alpha
    • Protein or peptide: DNA-directed RNA polymerase subunit beta
    • Protein or peptide: DNA-directed RNA polymerase subunit beta'
    • Protein or peptide: DNA-directed RNA polymerase subunit omega
    • Protein or peptide: RNA polymerase sigma factor SigA
    • Protein or peptide: RNA polymerase-binding protein RbpA
    • DNA: DNA (65-MER)
    • DNA: DNA (65-MER)
    • Protein or peptide: RNA polymerase-binding transcription factor CarD
  • Ligand: ZINC ION
  • Ligand: MAGNESIUM ION

+
Supramolecule #1: Mycobacterium tuberculosis RNAP open promoter complex

SupramoleculeName: Mycobacterium tuberculosis RNAP open promoter complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#9
Source (natural)Organism: Mycobacterium tuberculosis (bacteria)

+
Macromolecule #1: DNA-directed RNA polymerase subunit alpha

MacromoleculeName: DNA-directed RNA polymerase subunit alpha / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO / EC number: DNA-directed RNA polymerase
Source (natural)Organism: Mycobacterium tuberculosis (bacteria)
Molecular weightTheoretical: 37.745328 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MLISQRPTLS EDVLTDNRSQ FVIEPLEPGF GYTLGNSLRR TLLSSIPGAA VTSIRIDGVL HEFTTVPGVK EDVTEIILNL KSLVVSSEE DEPVTMYLRK QGPGEVTAGD IVPPAGVTVH NPGMHIATLN DKGKLEVELV VERGRGYVPA VQNRASGAEI G RIPVDSIY ...String:
MLISQRPTLS EDVLTDNRSQ FVIEPLEPGF GYTLGNSLRR TLLSSIPGAA VTSIRIDGVL HEFTTVPGVK EDVTEIILNL KSLVVSSEE DEPVTMYLRK QGPGEVTAGD IVPPAGVTVH NPGMHIATLN DKGKLEVELV VERGRGYVPA VQNRASGAEI G RIPVDSIY SPVLKVTYKV DATRVEQRTD FDKLILDVET KNSISPRDAL ASAGKTLVEL FGLARELNVE AEGIEIGPSP AE ADHIASF ALPIDDLDLT VRSYNCLKRE GVHTVGELVA RTESDLLDIR NFGQKSIDEV KIKLHQLGLS LKDSPPSFDP SEV AGYDVA TGTWSTEGAY DEQDYAETEQ L

UniProtKB: DNA-directed RNA polymerase subunit alpha

+
Macromolecule #2: DNA-directed RNA polymerase subunit beta

MacromoleculeName: DNA-directed RNA polymerase subunit beta / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-directed RNA polymerase
Source (natural)Organism: Mycobacterium tuberculosis (bacteria)
Molecular weightTheoretical: 125.390875 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MADSRQSKTA ASPSPSRPQS SSNNSVPGAP NRVSFAKLRE PLEVPGLLDV QTDSFEWLIG SPRWRESAAE RGDVNPVGGL EEVLYELSP IEDFSGSMSL SFSDPRFDDV KAPVDECKDK DMTYAAPLFV TAEFINNNTG EIKSQTVFMG DFPMMTEKGT F IINGTERV ...String:
MADSRQSKTA ASPSPSRPQS SSNNSVPGAP NRVSFAKLRE PLEVPGLLDV QTDSFEWLIG SPRWRESAAE RGDVNPVGGL EEVLYELSP IEDFSGSMSL SFSDPRFDDV KAPVDECKDK DMTYAAPLFV TAEFINNNTG EIKSQTVFMG DFPMMTEKGT F IINGTERV VVSQLVRSPG VYFDETIDKS TDKTLHSVKV IPSRGAWLEF DVDKRDTVGV RIDRKRRQPV TVLLKALGWT SE QIVERFG FSEIMRSTLE KDNTVGTDEA LLDIYRKLRP GEPPTKESAQ TLLENLFFKE KRYDLARVGR YKVNKKLGLH VGE PITSST LTEEDVVATI EYLVRLHEGQ TTMTVPGGVE VPVETDDIDH FGNRRLRTVG ELIQNQIRVG MSRMERVVRE RMTT QDVEA ITPQTLINIR PVVAAIKEFF GTSQLSQFMD QNNPLSGLTH KRRLSALGPG GLSRERAGLE VRDVHPSHYG RMCPI ETPE GPNIGLIGSL SVYARVNPFG FIETPYRKVV DGVVSDEIVY LTADEEDRHV VAQANSPIDA DGRFVEPRVL VRRKAG EVE YVPSSEVDYM DVSPRQMVSV ATAMIPFLEH DDANRALMGA NMQRQAVPLV RSEAPLVGTG MELRAAIDAG DVVVAEE SG VIEEVSADYI TVMHDNGTRR TYRMRKFARS NHGTCANQCP IVDAGDRVEA GQVIADGPCT DDGEMALGKN LLVAIMPW E GHNYEDAIIL SNRLVEEDVL TSIHIEEHEI DARDTKLGAE EITRDIPNIS DEVLADLDER GIVRIGAEVR DGDILVGKV TPKGETELTP EERLLRAIFG EKAREVRDTS LKVPHGESGK VIGIRVFSRE DEDELPAGVN ELVRVYVAQK RKISDGDKLA GRHGNKGVI GKILPVEDMP FLADGTPVDI ILNTHGVPRR MNIGQILETH LGWCAHSGWK VDAAKGVPDW AARLPDELLE A QPNAIVST PVFDGAQEAE LQGLLSCTLP NRDGDVLVDA DGKAMLFDGR SGEPFPYPVT VGYMYIMKLH HLVDDKIHAR ST GPYSMIT QQPLGGKAQF GGQRFGEMEC WAMQAYGAAY TLQELLTIKS DDTVGRVKVY EAIVKGENIP EPGIPESFKV LLK ELQSLC LNVEVLSS

UniProtKB: DNA-directed RNA polymerase subunit beta

+
Macromolecule #3: DNA-directed RNA polymerase subunit beta'

MacromoleculeName: DNA-directed RNA polymerase subunit beta' / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-directed RNA polymerase
Source (natural)Organism: Mycobacterium tuberculosis (bacteria)
Molecular weightTheoretical: 152.882109 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: DGAAIELREG EDEDLERAAA NLGINLSRNE SASVEDLALA RHGGSGAMLD VNFFDELRIG LATAEDIRQW SYGEVKKPET INYRTLKPE KDGLFCEKIF GPTRDWECYC GKYKRVRFKG IICERCGVEV TRAKVRRERM GHIELAAPVT HIWYFKGVPS R LGYLLDLA ...String:
DGAAIELREG EDEDLERAAA NLGINLSRNE SASVEDLALA RHGGSGAMLD VNFFDELRIG LATAEDIRQW SYGEVKKPET INYRTLKPE KDGLFCEKIF GPTRDWECYC GKYKRVRFKG IICERCGVEV TRAKVRRERM GHIELAAPVT HIWYFKGVPS R LGYLLDLA PKDLEKIIYF AAYVITSVDE EMRHNELSTL EAEMAVERKA VEDQRDGELE ARAQKLEADL AELEAEGAKA DA RRKVRDG GEREMRQIRD RAQRELDRLE DIWSTFTKLA PKQLIVDENL YRELVDRYGE YFTGAMGAES IQKLIENFDI DAE AESLRD VIRNGKGQKK LRALKRLKVV AAFQQSGNSP MGMVLDAVPV IPPELRPMVQ LDGGRFATSD LNDLYRRVIN RNNR LKRLI DLGAPEIIVN NEKRMLQESV DALFDNGRRG RPVTGPGNRP LKSLSDLLKG KQGRFRQNLL GKRVDYSGRS VIVVG PQLK LHQCGLPKLM ALELFKPFVM KRLVDLNHAQ NIKSAKRMVE RQRPQVWDVL EEVIAEHPVL LNRAPTLHRL GIQAFE PML VEGKAIQLHP LVCEAFNADF DGDQMAVHLP LSAEAQAEAR ILMLSSNNIL SPASGRPLAM PRLDMVTGLY YLTTEVP GD TGEYQPASGD HPETGVYSSP AEAIMAADRG VLSVRAKIKV RLTQLRPPVE IEAELFGHSG WQPGDAWMAE TTLGRVMF N ELLPLGYPFV NKQMHKKVQA AIINDLAERY PMIVVAQTVD KLKDAGFYWA TRSGVTVSMA DVLVPPRKKE ILDHYEERA DKVEKQFQRG ALNHDERNEA LVEIWKEATD EVGQALREHY PDDNPIITIV DSGATGNFTQ TRTLAGMKGL VTNPKGEFIP RPVKSSFRE GLTVLEYFIN THGARKGLAD TALRTADSGY LTRRLVDVSQ DVIVREHDCQ TERGIVVELA ERAPDGTLIR D PYIETSAY ARTLGTDAVD EAGNVIVERG QDLGDPEIDA LLAAGITQVK VRSVLTCATS TGVCATCYGR SMATGKLVDI GE AVGIVAA QSIGEPGTQL TMRTFHQGGV GEDITGGLPR VQELFEARVP RGKAPIADVT GRVRLEDGER FYKITIVPDD GGE EVVYDK ISKRQRLRVF KHEDGSERVL SDGDHVEVGQ QLMEGSADPH EVLRVQGPRE VQIHLVREVQ EVYRAQGVSI HDKH IEVIV RQMLRRVTII DSGSTEFLPG SLIDRAEFEA ENRRVVAEGG EPAAGRPVLM GITKASLATD SWLSAASFQE TTRVL TDAA INCRSDKLNG LKENVIIGKL IPAGTGINRY RNIAVQPTEE ARAAAYTIPS YEDQYYSPDF GAATGAAVPL DDYGYS DYR HHHHHHHH

UniProtKB: DNA-directed RNA polymerase subunit beta'

+
Macromolecule #4: DNA-directed RNA polymerase subunit omega

MacromoleculeName: DNA-directed RNA polymerase subunit omega / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-directed RNA polymerase
Source (natural)Organism: Mycobacterium tuberculosis (bacteria)
Molecular weightTheoretical: 11.776996 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
GSISQSDASL AAVPAVDQFD PSSGASGGYD TPLGITNPPI DELLDRVSSK YALVIYAAKR ARQINDYYNQ LGEGILEYVG PLVEPGLQE KPLSIALREI HADLLEHTEG E

UniProtKB: DNA-directed RNA polymerase subunit omega

+
Macromolecule #5: RNA polymerase sigma factor SigA

MacromoleculeName: RNA polymerase sigma factor SigA / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mycobacterium tuberculosis (bacteria)
Molecular weightTheoretical: 58.169477 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: GPHMAATKAS TATDEPVKRT ATKSPAASAS GAKTGAKRTA AKSASGSPPA KRATKPAARS VKPASAPQDT TTSTIPKRKT RAAAKSAAA KAPSARGHAT KPRAPKDAQH EAATDPEDAL DSVEELDAEP DLDVEPGEDL DLDAADLNLD DLEDDVAPDA D DDLDSGDD ...String:
GPHMAATKAS TATDEPVKRT ATKSPAASAS GAKTGAKRTA AKSASGSPPA KRATKPAARS VKPASAPQDT TTSTIPKRKT RAAAKSAAA KAPSARGHAT KPRAPKDAQH EAATDPEDAL DSVEELDAEP DLDVEPGEDL DLDAADLNLD DLEDDVAPDA D DDLDSGDD EDHEDLEAEA AVAPGQTADD DEEIAEPTEK DKASGDFVWD EDESEALRQA RKDAELTASA DSVRAYLKQI GK VALLNAE EEVELAKRIE AGLYATQLMT ELSERGEKLP AAQRRDMMWI CRDGDRAKNH LLEANLRLVV SLAKRYTGRG MAF LDLIQE GNLGLIRAVE KFDYTKGYKF STYATWWIRQ AITRAMADQA RTIRIPVHMV EVINKLGRIQ RELLQDLGRE PTPE ELAKE MDITPEKVLE IQQYAREPIS LDQTIGDEGD SQLGDFIEDS EAVVAVDAVS FTLLQDQLQS VLDTLSEREA GVVRL RFGL TDGQPRTLDE IGQVYGVTRE RIRQIESKTM SKLRHPSRSQ VLRDYLD

UniProtKB: RNA polymerase sigma factor SigA

+
Macromolecule #6: RNA polymerase-binding protein RbpA

MacromoleculeName: RNA polymerase-binding protein RbpA / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mycobacterium tuberculosis (bacteria)
Molecular weightTheoretical: 12.993695 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MADRVLRGSR LGAVSYETDR NHDLAPRQIA RYRTDNGEEF EVPFADDAEI PGTWLCRNGM EGTLIEGDLP EPKKVKPPRT HWDMLLERR SIEELEELLK ERLELIRSRR RG

UniProtKB: RNA polymerase-binding protein RbpA

+
Macromolecule #9: RNA polymerase-binding transcription factor CarD

MacromoleculeName: RNA polymerase-binding transcription factor CarD / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mycobacterium tuberculosis (bacteria)
Molecular weightTheoretical: 17.933361 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MIFKVGDTVV YPHHGAALVE AIETRTIKGE QKEYLVLKVA QGDLTVRVPA ENAEYVGVRD VVGQEGLDKV FQVLRAPHTE EPTNWSRRY KANLEKLASG DVNKVAEVVR DLWRRDQERG LSAGEKRMLA KARQILVGEL ALAESTDDAK AETILDEVLA A AS

UniProtKB: RNA polymerase-binding transcription factor CarD

+
Macromolecule #7: DNA (65-MER)

MacromoleculeName: DNA (65-MER) / type: dna / ID: 7 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Mycobacterium tuberculosis (bacteria)
Molecular weightTheoretical: 27.907809 KDa
SequenceString: (DG)(DG)(DC)(DT)(DA)(DT)(DG)(DG)(DA)(DT) (DG)(DA)(DC)(DC)(DG)(DA)(DA)(DC)(DC)(DT) (DG)(DG)(DT)(DC)(DT)(DT)(DG)(DA)(DC) (DT)(DC)(DC)(DA)(DT)(DT)(DG)(DC)(DC)(DG) (DG) (DA)(DT)(DT)(DT)(DG)(DT) ...String:
(DG)(DG)(DC)(DT)(DA)(DT)(DG)(DG)(DA)(DT) (DG)(DA)(DC)(DC)(DG)(DA)(DA)(DC)(DC)(DT) (DG)(DG)(DT)(DC)(DT)(DT)(DG)(DA)(DC) (DT)(DC)(DC)(DA)(DT)(DT)(DG)(DC)(DC)(DG) (DG) (DA)(DT)(DT)(DT)(DG)(DT)(DA)(DT) (DT)(DA)(DG)(DA)(DC)(DT)(DG)(DG)(DC)(DA) (DG)(DG) (DG)(DT)(DT)(DG)(DC)(DC)(DC) (DC)(DG)(DA)(DA)(DG)(DC)(DG)(DG)(DG)(DC) (DG)(DG)(DA) (DA)(DA)(DC)(DA)(DA)(DG) (DC)(DA)(DC)(DG)

+
Macromolecule #8: DNA (65-MER)

MacromoleculeName: DNA (65-MER) / type: dna / ID: 8 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Mycobacterium tuberculosis (bacteria)
Molecular weightTheoretical: 27.618625 KDa
SequenceString: (DC)(DG)(DT)(DG)(DC)(DT)(DT)(DG)(DT)(DT) (DT)(DC)(DC)(DG)(DC)(DC)(DC)(DG)(DC)(DT) (DT)(DC)(DG)(DG)(DG)(DG)(DC)(DA)(DA) (DC)(DC)(DC)(DT)(DG)(DC)(DC)(DA)(DG)(DT) (DC) (DT)(DA)(DA)(DT)(DA)(DC) ...String:
(DC)(DG)(DT)(DG)(DC)(DT)(DT)(DG)(DT)(DT) (DT)(DC)(DC)(DG)(DC)(DC)(DC)(DG)(DC)(DT) (DT)(DC)(DG)(DG)(DG)(DG)(DC)(DA)(DA) (DC)(DC)(DC)(DT)(DG)(DC)(DC)(DA)(DG)(DT) (DC) (DT)(DA)(DA)(DT)(DA)(DC)(DA)(DA) (DA)(DT)(DC)(DC)(DG)(DG)(DC)(DA)(DA)(DT) (DG)(DG) (DA)(DG)(DT)(DC)(DA)(DA)(DG) (DA)(DC)(DC)(DA)(DG)(DG)(DT)(DT)(DC)(DG) (DG)(DT)(DC) (DA)(DT)(DC)(DC)(DA)(DT) (DA)(DG)(DC)(DC)

+
Macromolecule #10: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 10 / Number of copies: 2 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

+
Macromolecule #11: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 11 / Number of copies: 1 / Formula: MG
Molecular weightTheoretical: 24.305 Da

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 8
GridDetails: unspecified
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 69.9 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

Startup modelType of model: INSILICO MODEL
Final reconstructionNumber images used: 211381
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: PROJECTION MATCHING

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
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

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • 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

Read more