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- EMDB-21365: Anthrax octamer prechannel bound to full-length edema factor -

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Basic information

Entry
Database: EMDB / ID: EMD-21365
TitleAnthrax octamer prechannel bound to full-length edema factor
Map data
Sample
  • Complex: Anthrax octamer prechannel bound to full-length edema factor
    • Protein or peptide: Protective antigen
    • Protein or peptide: Protective antigen
    • Protein or peptide: Calmodulin-sensitive adenylate cyclase
  • Ligand: CALCIUM ION
Keywordstranslocase / anthrax toxin / protective antigen / edema factor / octamer
Function / homology
Function and homology information


positive regulation of apoptotic process in another organism / calcium- and calmodulin-responsive adenylate cyclase activity / : / adenylate cyclase / cAMP biosynthetic process / adenylate cyclase activity / host cell cytosol / negative regulation of MAPK cascade / Uptake and function of anthrax toxins / catalytic complex ...positive regulation of apoptotic process in another organism / calcium- and calmodulin-responsive adenylate cyclase activity / : / adenylate cyclase / cAMP biosynthetic process / adenylate cyclase activity / host cell cytosol / negative regulation of MAPK cascade / Uptake and function of anthrax toxins / catalytic complex / small molecule binding / host cell endosome membrane / protein homooligomerization / metallopeptidase activity / toxin activity / calmodulin binding / host cell plasma membrane / extracellular region / ATP binding / identical protein binding / membrane / metal ion binding
Similarity search - Function
: / Oedema factor (EF), alpha-helical domain / Protective antigen domain 4 / : / Anthrax protective antigen, immunoglobulin-like domain / Anthrax toxin, edema factor, central / Anthrax toxin, edema factor, C-terminal / Anthrax toxin, edema factor, central domain superfamily / Anthrax toxin LF subunit / Anthrax toxin, lethal/endema factor ...: / Oedema factor (EF), alpha-helical domain / Protective antigen domain 4 / : / Anthrax protective antigen, immunoglobulin-like domain / Anthrax toxin, edema factor, central / Anthrax toxin, edema factor, C-terminal / Anthrax toxin, edema factor, central domain superfamily / Anthrax toxin LF subunit / Anthrax toxin, lethal/endema factor / : / Anthrax toxin lethal factor (ATLF)-like domain profile. / Anthrax toxin, lethal/endema factor, N-/C-terminal / Anthrax toxin lethal factor, N- and C-terminal domain / Bacterial exotoxin B / Protective antigen, heptamerisation domain / Protective antigen, Ca-binding domain / Clostridial binary toxin B/anthrax toxin PA, domain 3 / Protective antigen, heptamerisation domain superfamily / Clostridial binary toxin B/anthrax toxin PA Ca-binding domain / Clostridial binary toxin B/anthrax toxin PA domain 2 / Clostridial binary toxin B/anthrax toxin PA domain 3 / PA14/GLEYA domain / PA14 domain profile. / PA14 domain / PA14 / PA14 domain / Metallopeptidase, catalytic domain superfamily
Similarity search - Domain/homology
Protective antigen / Calmodulin-sensitive adenylate cyclase
Similarity search - Component
Biological speciesBacillus anthracis (anthrax bacterium)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.3 Å
AuthorsZhou K / Hardenbrook NJ
Funding support United States, 3 items
OrganizationGrant numberCountry
National Science Foundation (NSF, United States)DMR-1548924 United States
National Institutes of Health/National Library of Medicine (NIH/NLM)R01GM071940/AI094386/DE025567 United States
National Institutes of Health/National Library of Medicine (NIH/NLM)R21AI124020 United States
CitationJournal: Structure / Year: 2020
Title: Atomic Structures of Anthrax Prechannel Bound with Full-Length Lethal and Edema Factors.
Authors: Kang Zhou / Shiheng Liu / Nathan J Hardenbrook / Yanxiang Cui / Bryan A Krantz / Z Hong Zhou /
Abstract: Pathogenesis of anthrax disease involves two cytotoxic enzymes-edema factor (EF) and lethal factor (LF)-which are individually recruited by the protective antigen heptamer (PA) or octamer (PA) ...Pathogenesis of anthrax disease involves two cytotoxic enzymes-edema factor (EF) and lethal factor (LF)-which are individually recruited by the protective antigen heptamer (PA) or octamer (PA) prechannel and subsequently translocated across channels formed on the endosomal membrane upon exposure to low pH. Here, we report the atomic structures of PA prechannel-bound full-length EF and LF. In this pretranslocation state, the N-terminal segment of both factors refolds into an α helix engaged in the α clamp of the prechannel. Recruitment to the PA prechannel exposes an originally buried β strand of both toxins and enables domain organization of EF. Many interactions occur on domain interfaces in both PA prechannel-bound EF and LF, leading to toxin compaction prior to translocation. Our results provide key insights into the molecular mechanisms of translocation-coupled protein unfolding and translocation.
History
DepositionFeb 7, 2020-
Header (metadata) releaseDec 16, 2020-
Map releaseDec 16, 2020-
UpdateMar 6, 2024-
Current statusMar 6, 2024Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.016
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by cylindrical radius
  • Surface level: 0.016
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6vra
  • Surface level: 0.016
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_21365.png

Downloads & links

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Map

FileDownload / File: emd_21365.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.07 Å
Density
Contour LevelBy AUTHOR: 0.016 / Movie #1: 0.016
Minimum - Maximum-0.07110073 - 0.15735517
Average (Standard dev.)0.0005696753 (±0.004965833)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions300300300
Spacing300300300
CellA=B=C: 321.00003 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.071.071.07
M x/y/z300300300
origin x/y/z0.0000.0000.000
length x/y/z321.000321.000321.000
α/β/γ90.00090.00090.000
start NX/NY/NZ1081340
NX/NY/NZ13584349
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS300300300
D min/max/mean-0.0710.1570.001

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Supplemental data

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Sample components

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Entire : Anthrax octamer prechannel bound to full-length edema factor

EntireName: Anthrax octamer prechannel bound to full-length edema factor
Components
  • Complex: Anthrax octamer prechannel bound to full-length edema factor
    • Protein or peptide: Protective antigen
    • Protein or peptide: Protective antigen
    • Protein or peptide: Calmodulin-sensitive adenylate cyclase
  • Ligand: CALCIUM ION

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Supramolecule #1: Anthrax octamer prechannel bound to full-length edema factor

SupramoleculeName: Anthrax octamer prechannel bound to full-length edema factor
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3
Source (natural)Organism: Bacillus anthracis (anthrax bacterium)
Molecular weightTheoretical: 860 kDa/nm

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Macromolecule #1: Protective antigen

MacromoleculeName: Protective antigen / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Bacillus anthracis (anthrax bacterium)
Molecular weightTheoretical: 82.511336 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: QENRLLNESE SSSQGLLGYY FSDLNFQAPM VVTSSTTGDL SIPSSELENI PSENQYFQSA IWSGFIKVKK SDEYTFATSA DNHVTMWVD DQEVINKASN SNKIRLEKGR LYQIKIQYQR EDPTEKGLDF KLYWTDSQNK KEVISSDNLQ LPELKQKSSN S LEVLFQGS ...String:
QENRLLNESE SSSQGLLGYY FSDLNFQAPM VVTSSTTGDL SIPSSELENI PSENQYFQSA IWSGFIKVKK SDEYTFATSA DNHVTMWVD DQEVINKASN SNKIRLEKGR LYQIKIQYQR EDPTEKGLDF KLYWTDSQNK KEVISSDNLQ LPELKQKSSN S LEVLFQGS TSAGPTVPDR DNDGIPDSLE VEGYTVDVKN KRTFLSPWIS NIHEKKGLTK YKSSPEKWST ASDPYSDFEK VT GRIDGNV SPEANHPLVA AYPIVHVDME NIILSKNEDQ STQNTDSQTR TISKNTSTSR THTSEVHGNA EVHASFFDIG GSV SAGFSN SNSSTVAIDH SLSLAGERTW AETMGLNTAD TARLNANIRY VNTGTAPIYN VLPTTSLVLG KNQTLATIKA KENQ LSQIL APNNYYPSKN LAPIALNAQD DFSSTPITMN YNQFLELEKT KQLRLDTDQV YGNIATYNFE NGRVRVDTGS NWSEV LPQI QETTARIIFN GKDLNLVERR IAAVNPSDPL ETTKPDMTLK EALKIAFGFN EPNGNLQYQG KDITEFDFNF DQQTSQ NIK NQLAELNATN IYTVLDKIKL NAKMNILIRD KRFHYDRNNI AVGADESVVK EAHREVINSS TEGLLLNIDK DIRKILS GY IVEIEDTEGL KEVINDRYDM LNISSLRQDG KTFIDFKKYN DKLPLYISNP NYKVNVYAVT KENTIINPSE NGDTSTNG I KKILIFSKKG YEIG

UniProtKB: Protective antigen

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Macromolecule #2: Protective antigen

MacromoleculeName: Protective antigen / type: protein_or_peptide / ID: 2 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Bacillus anthracis (anthrax bacterium)
Molecular weightTheoretical: 82.639672 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: QENRLLNESE SSSQGLLGYY FSDLNFQAPM VVTSSTTGDL SIPSSELENI PSENQYFQSA IWSGFIKVKK SDEYTFATSA DNHVTMWVD DQEVINKASN SNKIRLEKGR LYQIKIQYQR ENPTEKGLDF KLYWTDSQNK KEVISSDNLQ LPELKQKSSN S LEVLFQGS ...String:
QENRLLNESE SSSQGLLGYY FSDLNFQAPM VVTSSTTGDL SIPSSELENI PSENQYFQSA IWSGFIKVKK SDEYTFATSA DNHVTMWVD DQEVINKASN SNKIRLEKGR LYQIKIQYQR ENPTEKGLDF KLYWTDSQNK KEVISSDNLQ LPELKQKSSN S LEVLFQGS TSAGPTVPDR DNDGIPDSLE VEGYTVDVKN KRTFLSPWIS NIHEKKGLTK YKSSPEKWST ASDPYSDFEK VT GRIDKNV SPEARHPLVA AYPIVHVDME NIILSKNEDQ STQNTDSQTR TISKNTSTSR THTSEVHGNA EVHASFFDIG GSV SAGFSN SNSSTVAIDH SLSLAGERTW AETMGLNTAD TARLNANIRY VNTGTAPIYN VLPTTSLVLG KNQTLATIKA KENQ LSQIL APNNYYPSKN LAPIALNAQD DFSSTPITMN YNQFLELEKT KQLRLDTDQV YGNIATYNFE NGRVRVDTGS NWSEV LPQI QETTARIIFN GKDLNLVERR IAAVNPSKPL ETTKPDMTLK EALKIAFGFN EPNGNLQYQG KDITEFDFNF DQQTSQ NIK NQLAELNATN IYTVLDKIKL NAKMNILIRD KRFHYDRNNI AVGADESVVK EAHREVINSS TEGLLLNIDK DIRKILS GY IVEIEDTEGL KEVINDRYDM LNISSLRQDG KTFIDFKKYN DKLPLYISNP NYKVNVYAVT KENTIINPSE NGDTSTNG I KKILIFSKKG YEIG

UniProtKB: Protective antigen

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Macromolecule #3: Calmodulin-sensitive adenylate cyclase

MacromoleculeName: Calmodulin-sensitive adenylate cyclase / type: protein_or_peptide / ID: 3 / Number of copies: 4 / Enantiomer: LEVO / EC number: adenylate cyclase
Source (natural)Organism: Bacillus anthracis (anthrax bacterium)
Molecular weightTheoretical: 88.955578 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: MNEHYTESDI KRNHKTEKNK TEKEKFKDSI NNLVKTEFTN ETLDKIQQTQ DLLKKIPKDV LEIYSELGGE IYFTDIDLVE HKELQDLSE EEKNSMNSRG EKVPFASRFV FEKKRETPKL IINIKDYAIN SEQSKEVYYE IGKGISLDII SKDKSLDPEF L NLIKSLSD ...String:
MNEHYTESDI KRNHKTEKNK TEKEKFKDSI NNLVKTEFTN ETLDKIQQTQ DLLKKIPKDV LEIYSELGGE IYFTDIDLVE HKELQDLSE EEKNSMNSRG EKVPFASRFV FEKKRETPKL IINIKDYAIN SEQSKEVYYE IGKGISLDII SKDKSLDPEF L NLIKSLSD DSDSSDLLFS QKFKEKLELN NKSIDINFIK ENLTEFQHAF SLAFSYYFAP DHRTVLELYA PDMFEYMNKL EK GGFEKIS ESLKKEGVEK DRIDVLKGEK ALKASGLVPE HADAFKKIAR ELNTYILFRP VNKLATNLIK SGVATKGLNV HGK SSDWGP VAGYIPFDQD LSKKHGQQLA VEKGNLENKK SITEHEGEIG KIPLKLDHLR IEELKENGII LKGKKEIDNG KKYY LLESN NQVYEFRISD ENNEVQYKTK EGKITVLGEK FNWRNIEVMA KNVEGVLKPL TADYDLFALA PSLTEIKKQI PQKEW DKVV NTPNSLEKQK GVTNLLIKYG IERKPDSTKG TLSNWQKQML DRLNEAVKYT GYTGGDVVNH GTEQDNEEFP EKDNEI FII NPEGEFILTK NWEMTGRFIE KNITGKDYLY YFNRSYNKIA PGNKAYIEWT DPITKAKINT IPTSAEFIKN LSSIRRS SN VGVYKDSGDK DEFAKKESVK KIAGYLSDYY NSANHIFSQE KKRKISIFRG IQAYNEIENV LKSKQIAPEY KNYFQYLK E RITNQVQLLL THQKSNIEFK LLYKQLNFTE NETDNFEVFQ KIIDEK

UniProtKB: Calmodulin-sensitive adenylate cyclase

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Macromolecule #4: CALCIUM ION

MacromoleculeName: CALCIUM ION / type: ligand / ID: 4 / Number of copies: 16 / Formula: CA
Molecular weightTheoretical: 40.078 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
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 62.9 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

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Image processing

Startup modelType of model: EMDB MAP
EMDB ID:

6224

Final reconstructionApplied symmetry - Point group: C4 (4 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.0) / Number images used: 78465
Initial angle assignmentType: ANGULAR RECONSTITUTION / Software - Name: RELION (ver. 3.0)
Final angle assignmentType: ANGULAR RECONSTITUTION / Software - Name: RELION (ver. 3.0)
Final 3D classificationSoftware - Name: RELION (ver. 3.0)

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