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- EMDB-21408: Mycobacterium tuberculosis RNAP S456L mutant transcription initia... -

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Basic information

Entry
Database: EMDB / ID: EMD-21408
TitleMycobacterium tuberculosis RNAP S456L mutant transcription initiation intermediate structure with Sorangicin
Map dataMycobacterium tuberculosis RNAP S456L mutant transcription initiation intermediate structure with Sorangicin
Sample
  • Complex: Mycobacterium tuberculosis RNAP S456L mutant promoter melting intermediate complex
    • Protein or peptide: x 7 types
    • DNA: x 2 types
  • Ligand: x 3 types
Keywordsinitiation / transcription bubble / antibiotic / sorangicin / open promoter complex / TRANSCRIPTION / TRANSFERASE-DNA-ANTIBIOTIC complex
Function / homology
Function and homology information


response to water / bacterial-type RNA polymerase holo enzyme binding / Antimicrobial action and antimicrobial resistance in Mtb / sigma factor activity / rRNA transcription / bacterial-type RNA polymerase core enzyme binding / cytosolic DNA-directed RNA polymerase complex / DNA-directed RNA polymerase complex / peptidoglycan-based cell wall / DNA-templated transcription initiation ...response to water / bacterial-type RNA polymerase holo enzyme binding / Antimicrobial action and antimicrobial resistance in Mtb / sigma factor activity / rRNA transcription / bacterial-type RNA polymerase core enzyme binding / cytosolic DNA-directed RNA polymerase complex / DNA-directed RNA polymerase complex / peptidoglycan-based cell wall / DNA-templated transcription initiation / ribonucleoside binding / DNA-directed RNA polymerase / DNA-directed RNA polymerase activity / 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 / cytoplasm / cytosol
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 beta subunit, bacterial-type / DNA-directed RNA polymerase, alpha subunit / DNA-directed RNA polymerase, subunit beta-prime / RNA polymerase Rpb6 / RNA polymerase, subunit omega/Rpo6/RPB6 / RNA polymerase Rpb6 / RNA polymerase Rpb2, domain 2 superfamily / RNA polymerase Rpb1, domain 3 superfamily / RPB6/omega subunit-like superfamily / 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 Rpb1, clamp domain superfamily / RNA polymerase Rpb1, domain 3 / RNA polymerase Rpb1, domain 3 / RNA polymerase Rpb1, domain 1 / RNA polymerase Rpb1, domain 1 / RNA polymerase, beta subunit, protrusion / RNA polymerase beta subunit / 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 / DNA-directed RNA polymerase, insert domain superfamily / RNA polymerase, N-terminal / RNA polymerase Rpb2, domain 2 / RNA polymerase Rpb1, funnel domain superfamily / RNA polymerase Rpb2, domain 2 / RNA polymerase I subunit A N-terminus / RNA polymerase, RBP11-like subunit / 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 / Resolution: 3.72 Å
AuthorsLilic M / Boyaci H
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) United States
CitationJournal: Proc Natl Acad Sci U S A / Year: 2020
Title: The antibiotic sorangicin A inhibits promoter DNA unwinding in a rifampicin-resistant RNA polymerase.
Authors: Mirjana Lilic / James Chen / Hande Boyaci / Nathaniel Braffman / Elizabeth A Hubin / Jennifer Herrmann / Rolf Müller / Rachel Mooney / Robert Landick / Seth A Darst / Elizabeth A Campbell /
Abstract: Rifampicin (Rif) is a first-line therapeutic used to treat the infectious disease tuberculosis (TB), which is caused by the pathogen (). The emergence of Rif-resistant (Rif) presents a need for new ...Rifampicin (Rif) is a first-line therapeutic used to treat the infectious disease tuberculosis (TB), which is caused by the pathogen (). The emergence of Rif-resistant (Rif) presents a need for new antibiotics. Rif targets the enzyme RNA polymerase (RNAP). Sorangicin A (Sor) is an unrelated inhibitor that binds in the Rif-binding pocket of RNAP. Sor inhibits a subset of Rif RNAPs, including the most prevalent clinical Rif RNAP substitution found in infected patients (S456>L of the β subunit). Here, we present structural and biochemical data demonstrating that Sor inhibits the wild-type RNAP by a similar mechanism as Rif: by preventing the translocation of very short RNAs. By contrast, Sor inhibits the Rif S456L enzyme at an earlier step, preventing the transition of a partially unwound promoter DNA intermediate to the fully opened DNA and blocking the template-strand DNA from reaching the active site in the RNAP catalytic center. By defining template-strand blocking as a mechanism for inhibition, we provide a mechanistic drug target in RNAP. Our finding that Sor inhibits the wild-type and mutant RNAPs through different mechanisms prompts future considerations for designing antibiotics against resistant targets. Also, we show that Sor has a better pharmacokinetic profile than Rif, making it a suitable starting molecule to design drugs to be used for the treatment of TB patients with comorbidities who require multiple medications.
History
DepositionFeb 18, 2020-
Header (metadata) releaseMar 18, 2020-
Map releaseOct 21, 2020-
UpdateMay 21, 2025-
Current statusMay 21, 2025Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.45
  • Imaged by UCSF Chimera
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  • Surface view colored by radius
  • Surface level: 0.45
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6vvz
  • Surface level: 0.45
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_21408.png

Downloads & links

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Map

FileDownload / File: emd_21408.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationMycobacterium tuberculosis RNAP S456L mutant transcription initiation intermediate structure with Sorangicin
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.3 Å/pix.
x 256 pix.
= 332.8 Å		1.3 Å/pix.
x 256 pix.
= 332.8 Å		1.3 Å/pix.
x 256 pix.
= 332.8 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

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.394 / Movie #1: 0.45
Minimum - Maximum-0.71056014 - 2.0375268
Average (Standard dev.)0.0038867793 (±0.08918184)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 332.8 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.31.31.3
M x/y/z256256256
origin x/y/z0.0000.0000.000
length x/y/z332.800332.800332.800
α/β/γ90.00090.00090.000
start NX/NY/NZ79740
NX/NY/NZ93103213
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS256256256
D min/max/mean-0.7112.0380.004

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Supplemental data

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Sample components

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Entire : Mycobacterium tuberculosis RNAP S456L mutant promoter melting int...

EntireName: Mycobacterium tuberculosis RNAP S456L mutant promoter melting intermediate complex
Components
  • Complex: Mycobacterium tuberculosis RNAP S456L mutant promoter melting intermediate 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
    • Protein or peptide: RNA polymerase-binding transcription factor CarD
    • DNA: DNA (62-MER)
    • DNA: DNA (65-MER)
  • Ligand: SORANGICIN A
  • Ligand: ZINC ION
  • Ligand: MAGNESIUM ION

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Supramolecule #1: Mycobacterium tuberculosis RNAP S456L mutant promoter melting int...

SupramoleculeName: Mycobacterium tuberculosis RNAP S456L mutant promoter melting intermediate complex
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#9
Source (natural)Organism: Mycobacterium tuberculosis (bacteria)

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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

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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: 130.096875 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 KRRLLALGPG 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 LNVEVLSSDG AAIELREGED EDLERAAANL GINLSRNESA SVEDLALARH GGS

UniProtKB: DNA-directed RNA polymerase subunit beta

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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: 148.202219 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: GAMLDVNFFD ELRIGLATAE DIRQWSYGEV KKPETINYRT LKPEKDGLFC EKIFGPTRDW ECYCGKYKRV RFKGIICERC GVEVTRAKV RRERMGHIEL AAPVTHIWYF KGVPSRLGYL LDLAPKDLEK IIYFAAYVIT SVDEEMRHNE LSTLEAEMAV E RKAVEDQR ...String:
GAMLDVNFFD ELRIGLATAE DIRQWSYGEV KKPETINYRT LKPEKDGLFC EKIFGPTRDW ECYCGKYKRV RFKGIICERC GVEVTRAKV RRERMGHIEL AAPVTHIWYF KGVPSRLGYL LDLAPKDLEK IIYFAAYVIT SVDEEMRHNE LSTLEAEMAV E RKAVEDQR DGELEARAQK LEADLAELEA EGAKADARRK VRDGGEREMR QIRDRAQREL DRLEDIWSTF TKLAPKQLIV DE NLYRELV DRYGEYFTGA MGAESIQKLI ENFDIDAEAE SLRDVIRNGK GQKKLRALKR LKVVAAFQQS GNSPMGMVLD AVP VIPPEL RPMVQLDGGR FATSDLNDLY RRVINRNNRL KRLIDLGAPE IIVNNEKRML QESVDALFDN GRRGRPVTGP GNRP LKSLS DLLKGKQGRF RQNLLGKRVD YSGRSVIVVG PQLKLHQCGL PKLMALELFK PFVMKRLVDL NHAQNIKSAK RMVER QRPQ VWDVLEEVIA EHPVLLNRAP TLHRLGIQAF EPMLVEGKAI QLHPLVCEAF NADFDGDQMA VHLPLSAEAQ AEARIL MLS SNNILSPASG RPLAMPRLDM VTGLYYLTTE VPGDTGEYQP ASGDHPETGV YSSPAEAIMA ADRGVLSVRA KIKVRLT QL RPPVEIEAEL FGHSGWQPGD AWMAETTLGR VMFNELLPLG YPFVNKQMHK KVQAAIINDL AERYPMIVVA QTVDKLKD A GFYWATRSGV TVSMADVLVP PRKKEILDHY EERADKVEKQ FQRGALNHDE RNEALVEIWK EATDEVGQAL REHYPDDNP IITIVDSGAT GNFTQTRTLA GMKGLVTNPK GEFIPRPVKS SFREGLTVLE YFINTHGARK GLADTALRTA DSGYLTRRLV DVSQDVIVR EHDCQTERGI VVELAERAPD GTLIRDPYIE TSAYARTLGT DAVDEAGNVI VERGQDLGDP EIDALLAAGI T QVKVRSVL TCATSTGVCA TCYGRSMATG KLVDIGEAVG IVAAQSIGEP GTQLTMRTFH QGGVGEDITG GLPRVQELFE AR VPRGKAP IADVTGRVRL EDGERFYKIT IVPDDGGEEV VYDKISKRQR LRVFKHEDGS ERVLSDGDHV EVGQQLMEGS ADP HEVLRV QGPREVQIHL VREVQEVYRA QGVSIHDKHI EVIVRQMLRR VTIIDSGSTE FLPGSLIDRA EFEAENRRVV AEGG EPAAG RPVLMGITKA SLATDSWLSA ASFQETTRVL TDAAINCRSD KLNGLKENVI IGKLIPAGTG INRYRNIAVQ PTEEA RAAA YTIPSYEDQY YSPDFGAATG AAVPLDDYGY SDYRHHHHHH HH

UniProtKB: DNA-directed RNA polymerase subunit beta'

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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

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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

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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

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Macromolecule #7: RNA polymerase-binding transcription factor CarD

MacromoleculeName: RNA polymerase-binding transcription factor CarD / type: protein_or_peptide / ID: 7 / 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

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Macromolecule #8: DNA (62-MER)

MacromoleculeName: DNA (62-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)

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Macromolecule #9: DNA (65-MER)

MacromoleculeName: DNA (65-MER) / type: dna / ID: 9 / 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)

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Macromolecule #10: SORANGICIN A

MacromoleculeName: SORANGICIN A / type: ligand / ID: 10 / Number of copies: 1 / Formula: SRN
Molecular weightTheoretical: 807.02 Da
Chemical component information

ChemComp-SRN:
SORANGICIN A

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Macromolecule #11: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 11 / Number of copies: 2 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Macromolecule #12: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 12 / Number of copies: 1 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 8
GridDetails: unspecified
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 71.0 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

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: EMDB MAP
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.72 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 47371
Initial angle assignmentType: PROJECTION MATCHING
Final angle assignmentType: PROJECTION MATCHING

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