+Open data
-Basic information
Entry | Database: PDB / ID: 8spw | ||||||
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Title | PS3 F1 Rotorless, low ATP | ||||||
Components | (ATP synthase subunit ...) x 2 | ||||||
Keywords | TRANSLOCASE / ATPase / Membrane protein / electron transport | ||||||
Function / homology | Function and homology information proton-transporting ATP synthase complex, catalytic core F(1) / H+-transporting two-sector ATPase / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / ADP binding / ATP hydrolysis activity / ATP binding / plasma membrane Similarity search - Function | ||||||
Biological species | Bacillus sp. PS3 (bacteria) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.5 Å | ||||||
Authors | Sobti, M. / Stewart, A.G. | ||||||
Funding support | Australia, 1items
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Citation | Journal: Structure / Year: 2024 Title: The series of conformational states adopted by rotorless F-ATPase during its hydrolysis cycle. Authors: Meghna Sobti / Hiroshi Ueno / Simon H J Brown / Hiroyuki Noji / Alastair G Stewart / Abstract: FF ATP synthase interchanges phosphate transfer energy and proton motive force via a rotary catalytic mechanism and isolated F-ATPase subcomplexes can also hydrolyze ATP to generate rotation of their ...FF ATP synthase interchanges phosphate transfer energy and proton motive force via a rotary catalytic mechanism and isolated F-ATPase subcomplexes can also hydrolyze ATP to generate rotation of their central γ rotor subunit. As ATP is hydrolyzed, the F-ATPase cycles through a series of conformational states that mediates unidirectional rotation of the rotor. However, even in the absence of a rotor, the α and β subunits are still able to pass through a series of conformations, akin to those that generate rotation. Here, we use cryoelectron microscopy to establish the structures of these rotorless states. These structures indicate that cooperativity in this system is likely mediated by contacts between the β subunit lever domains, irrespective of the presence of the γ rotor subunit. These findings provide insight into how long-range information may be transferred in large biological systems. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8spw.cif.gz | 479.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8spw.ent.gz | 395 KB | Display | PDB format |
PDBx/mmJSON format | 8spw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8spw_validation.pdf.gz | 1.8 MB | Display | wwPDB validaton report |
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Full document | 8spw_full_validation.pdf.gz | 1.8 MB | Display | |
Data in XML | 8spw_validation.xml.gz | 81.3 KB | Display | |
Data in CIF | 8spw_validation.cif.gz | 119.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sp/8spw ftp://data.pdbj.org/pub/pdb/validation_reports/sp/8spw | HTTPS FTP |
-Related structure data
Related structure data | 40688MC 8spvC 8spxC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
-ATP synthase subunit ... , 2 types, 6 molecules ABCDEF
#1: Protein | Mass: 51875.262 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus sp. PS3 (bacteria) / Gene: uncA, atpA / Production host: Escherichia coli (E. coli) References: UniProt: A0A0M3VGF9, H+-transporting two-sector ATPase #2: Protein | Mass: 51683.727 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus sp. PS3 (bacteria) / Gene: uncD / Production host: Escherichia coli (E. coli) / References: UniProt: A0A0M4U1P9 |
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-Non-polymers , 4 types, 11 molecules
#3: Chemical | ChemComp-ATP / #4: Chemical | ChemComp-MG / #5: Chemical | ChemComp-ADP / | #6: Chemical | ChemComp-PO4 / | |
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-Details
Has ligand of interest | N |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: PS3 F1 Rotorless / Type: COMPLEX / Entity ID: #1-#2 / Source: RECOMBINANT |
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Source (natural) | Organism: Bacillus sp. PS3 (bacteria) |
Source (recombinant) | Organism: Escherichia coli (E. coli) |
Buffer solution | pH: 7 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 1000 nm / Nominal defocus min: 1000 nm |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K2 QUANTUM (4k x 4k) |
-Processing
CTF correction | Type: PHASE FLIPPING ONLY | ||||||||||||||||||||||||
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3D reconstruction | Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 119736 / Symmetry type: POINT | ||||||||||||||||||||||||
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