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- EMDB-20008: Autoinhibited E. coli ATP synthase state 3 - reprocessed -

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Basic information

Entry
Database: EMDB / ID: EMD-20008
TitleAutoinhibited E. coli ATP synthase state 3 - reprocessed
Map dataprimary map
Sample
  • Complex: ATP synthase
Biological speciesEscherichia coli (E. coli)
Methodsingle particle reconstruction / cryo EM / Resolution: 7.22 Å
AuthorsSobti M / Smits C / Wong AS / Ishmukhametov R / Stock D / Sandin S / Stewart AG
Funding support Australia, 1 items
OrganizationGrant numberCountry
National Health and Medical Research Council (Australia)1146403 Australia
CitationJournal: Elife / Year: 2019
Title: Cryo-EM reveals distinct conformations of ATP synthase on exposure to ATP.
Authors: Meghna Sobti / Robert Ishmukhametov / James C Bouwer / Anita Ayer / Cacang Suarna / Nicola J Smith / Mary Christie / Roland Stocker / Thomas M Duncan / Alastair G Stewart /
Abstract: ATP synthase produces the majority of cellular energy in most cells. We have previously reported cryo-EM maps of autoinhibited ATP synthase imaged without addition of nucleotide (Sobti et al. 2016), ...ATP synthase produces the majority of cellular energy in most cells. We have previously reported cryo-EM maps of autoinhibited ATP synthase imaged without addition of nucleotide (Sobti et al. 2016), indicating that the subunit ε engages the α, β and γ subunits to lock the enzyme and prevent functional rotation. Here we present multiple cryo-EM reconstructions of the enzyme frozen after the addition of MgATP to identify the changes that occur when this ε inhibition is removed. The maps generated show that, after exposure to MgATP, ATP synthase adopts a different conformation with a catalytic subunit changing conformation substantially and the ε C-terminal domain transitioning via an intermediate 'half-up' state to a condensed 'down' state. This work provides direct evidence for unique conformational states that occur in ATP synthase when ATP binding prevents the ε C-terminal domain from entering the inhibitory 'up' state.
History
DepositionMar 19, 2019-
Header (metadata) releaseJul 3, 2019-
Map releaseJul 3, 2019-
UpdateJul 3, 2019-
Current statusJul 3, 2019Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.853
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.853
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_20008.png

Downloads & links

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Map

FileDownload / File: emd_20008.map.gz / Format: CCP4 / Size: 59.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationprimary map
Voxel sizeX=Y=Z: 1.4 Å
Density
Contour LevelBy AUTHOR: 0.853 / Movie #1: 0.853
Minimum - Maximum-3.1766198 - 5.18497
Average (Standard dev.)0.006474031 (±0.17809667)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions250250250
Spacing250250250
CellA=B=C: 350.0 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.41.41.4
M x/y/z250250250
origin x/y/z0.0000.0000.000
length x/y/z350.000350.000350.000
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS250250250
D min/max/mean-3.1775.1850.006

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Supplemental data

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Sample components

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Entire : ATP synthase

EntireName: ATP synthase
Components
  • Complex: ATP synthase

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Supramolecule #1: ATP synthase

SupramoleculeName: ATP synthase / type: complex / ID: 1 / Parent: 0
Source (natural)Organism: Escherichia coli (E. coli)
Recombinant expressionOrganism: Escherichia coli (E. coli)
Molecular weightTheoretical: 558 KDa

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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
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy
Image recordingFilm or detector model: FEI FALCON II (4k x 4k) / Average electron dose: 1.45 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 7.22 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 53587

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