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- EMDB-20957: Anthrax toxin protective antigen channels bound to edema factor -

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Basic information

Entry
Database: EMDB / ID: EMD-20957
TitleAnthrax toxin protective antigen channels bound to edema factor
Map data
Sample
  • Complex: Anthrax toxin protective antigen channels bound to edema factor
    • Protein or peptide: Protective antigen
    • Protein or peptide: Calmodulin-sensitive adenylate cyclase
  • Ligand: CALCIUM ION
Keywordstranslocase / anthrax toxin / protective antigen / edema factor
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 / small molecule binding / 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 / small molecule binding / Uptake and function of anthrax toxins / catalytic complex / negative regulation of MAPK cascade / 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/endema factor, N-/C-terminal / : / Anthrax toxin lethal factor, N- and C-terminal domain / Anthrax toxin lethal factor (ATLF)-like domain profile. / 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: 3.4 Å
AuthorsHardenbrook NJ / Liu S
Funding support United States, 3 items
OrganizationGrant numberCountry
National Science Foundation (NSF, United States)DMR-1548924 United States
National Institutes of Health/National Center for Research Resources (NIH/NCRR)R01GM071940/AI094386/DE025567 United States
National Institutes of Health/National Center for Research Resources (NIH/NCRR)R21AI124020 United States
CitationJournal: Nat Commun / Year: 2020
Title: Atomic structures of anthrax toxin protective antigen channels bound to partially unfolded lethal and edema factors.
Authors: Nathan J Hardenbrook / Shiheng Liu / Kang Zhou / Koyel Ghosal / Z Hong Zhou / Bryan A Krantz /
Abstract: Following assembly, the anthrax protective antigen (PA) forms an oligomeric translocon that unfolds and translocates either its lethal factor (LF) or edema factor (EF) into the host cell. Here, we ...Following assembly, the anthrax protective antigen (PA) forms an oligomeric translocon that unfolds and translocates either its lethal factor (LF) or edema factor (EF) into the host cell. Here, we report the cryo-EM structures of heptameric PA channels with partially unfolded LF and EF at 4.6 and 3.1-Å resolution, respectively. The first α helix and β strand of LF and EF unfold and dock into a deep amphipathic cleft, called the α clamp, which resides at the interface of two PA monomers. The α-clamp-helix interactions exhibit structural plasticity when comparing the structures of lethal and edema toxins. EF undergoes a largescale conformational rearrangement when forming the complex with the channel. A critical loop in the PA binding interface is displaced for about 4 Å, leading to the weakening of the binding interface prior to translocation. These structures provide key insights into the molecular mechanisms of translocation-coupled protein unfolding and translocation.
History
DepositionNov 14, 2019-
Header (metadata) releaseJan 29, 2020-
Map releaseMar 4, 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: 0.03
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.03
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6uzd
  • Surface level: 0.03
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_20957.png

Downloads & links

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Map

FileDownload / File: emd_20957.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.07 Å/pix.
x 300 pix.
= 321. Å		1.07 Å/pix.
x 300 pix.
= 321. Å		1.07 Å/pix.
x 300 pix.
= 321. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.07 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.03 / Movie #1: 0.03
Minimum - Maximum-0.08165202 - 0.20097578
Average (Standard dev.)0.000361506 (±0.006953357)
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/NZ000
NX/NY/NZ512512512
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS300300300
D min/max/mean-0.0820.2010.000

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Supplemental data

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Sample components

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Entire : Anthrax toxin protective antigen channels bound to edema factor

EntireName: Anthrax toxin protective antigen channels bound to edema factor
Components
  • Complex: Anthrax toxin protective antigen channels bound to edema factor
    • Protein or peptide: Protective antigen
    • Protein or peptide: Calmodulin-sensitive adenylate cyclase
  • Ligand: CALCIUM ION

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Supramolecule #1: Anthrax toxin protective antigen channels bound to edema factor

SupramoleculeName: Anthrax toxin protective antigen channels bound to edema factor
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
Source (natural)Organism: Bacillus anthracis (anthrax bacterium)
Molecular weightTheoretical: 613 kDa/nm

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Macromolecule #1: Protective antigen

MacromoleculeName: Protective antigen / type: protein_or_peptide / ID: 1 / Number of copies: 7 / Enantiomer: LEVO
Source (natural)Organism: Bacillus anthracis (anthrax bacterium)
Molecular weightTheoretical: 82.768828 KDa
Recombinant expressionOrganism: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
SequenceString: EVKQENRLLN ESESSSQGLL GYYFSDLNFQ APMVVTSSTT GDLSIPSSEL ENIPSENQYF QSAIWSGFIK VKKSDEYTFA TSADNHVTM WVDDQEVINK ASNSNKIRLE KGRLYQIKIQ YQRENPTEKG LDFKLYWTDS QNKKEVISSD NLQLPELKQK S SNSRKKRS ...String:
EVKQENRLLN ESESSSQGLL GYYFSDLNFQ APMVVTSSTT GDLSIPSSEL ENIPSENQYF QSAIWSGFIK VKKSDEYTFA TSADNHVTM WVDDQEVINK ASNSNKIRLE KGRLYQIKIQ YQRENPTEKG LDFKLYWTDS QNKKEVISSD NLQLPELKQK S SNSRKKRS 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 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: Calmodulin-sensitive adenylate cyclase

MacromoleculeName: Calmodulin-sensitive adenylate cyclase / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO / EC number: adenylate cyclase
Source (natural)Organism: Bacillus anthracis (anthrax bacterium)
Molecular weightTheoretical: 88.955578 KDa
Recombinant expressionOrganism: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (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 #3: CALCIUM ION

MacromoleculeName: CALCIUM ION / type: ligand / ID: 3 / Number of copies: 14 / 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: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 2.1) / Number images used: 72864
Initial angle assignmentType: ANGULAR RECONSTITUTION / Software - Name: RELION (ver. 2.1)
Final angle assignmentType: ANGULAR RECONSTITUTION / Software - Name: RELION (ver. 2.1)
Final 3D classificationSoftware - Name: RELION (ver. 2.1)

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