› 6cp6

Electron Microscopy
3.6Å resolution

Monomer yeast ATP synthase (F1Fo) reconstituted in nanodisc.

Released:
DOI: 10.2210/pdb6cp6/pdb
PDB entry 6cp6 coloured by chain, front view.
PDB entry 6cp6 coloured by chain, side view.
PDB entry 6cp6 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
High-resolution cryo-EM analysis of the yeast ATP synthase in a lipid membrane.
Srivastava AP, Luo M, Zhou W, Symersky J, Bai D, Chambers MG, Faraldo-Gómez JD, Liao M, Mueller DM
Science 360 (2018)
PMID: 29650704
Related structures: EMD-7548

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O + 4 H(+)(Side 1) = ADP + phosphate + 4 H(+)(Side 2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero 27-mer (preferred)
PDBe Complex ID:
PDB-CPX-133628 (preferred)
Entry contents:
14 distinct polypeptide molecules
Macromolecules (14 distinct):
ATP synthase subunit 9, mitochondrial Chains: K, L, M, N, O, P, Q, R, S, T
Molecule details ›
Chains: K, L, M, N, O, P, Q, R, S, T
Length: 76 amino acids
Theoretical weight: 7.79 KDa
Source organism: Saccharomyces cerevisiae S288C
UniProt:
  • Canonical: P61829 (Residues: 1-76; Coverage: 100%)
Gene names: ATP9, OLI1, OLI3, PHO2, Q0130
Sequence domains: ATP synthase subunit C
Structure domains: F1F0 ATP synthase subunit C
ATP synthase subunit 5, mitochondrial Chain: Y
Molecule details ›
Chain: Y
Length: 195 amino acids
Theoretical weight: 20.9 KDa
Source organism: Saccharomyces cerevisiae S288C
UniProt:
  • Canonical: P09457 (Residues: 18-212; Coverage: 92%)
Gene names: ATP5, D9740.11, OSCP, YDR298C
Sequence domains: ATP synthase delta (OSCP) subunit
ATP synthase subunit alpha, mitochondrial Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 510 amino acids
Theoretical weight: 55.01 KDa
Source organism: Saccharomyces cerevisiae S288C
UniProt:
  • Canonical: P07251 (Residues: 36-545; Coverage: 94%)
Gene names: ATP1, YBL0827, YBL099W
Sequence domains:
ATP synthase subunit beta, mitochondrial Chains: D, E, F
Molecule details ›
Chains: D, E, F
Length: 478 amino acids
Theoretical weight: 51.18 KDa
Source organism: Saccharomyces cerevisiae S288C
UniProt:
  • Canonical: P00830 (Residues: 34-511; Coverage: 94%)
Gene names: ATP2, J2041, YJR121W
Sequence domains:
Structure domains:
ATP synthase subunit gamma, mitochondrial Chain: G
Molecule details ›
Chain: G
Length: 278 amino acids
Theoretical weight: 30.66 KDa
Source organism: Saccharomyces cerevisiae S288C
UniProt:
  • Canonical: P38077 (Residues: 34-311; Coverage: 89%)
Gene names: ATP3, ATP3a, ATP3b, YBR039W, YBR0408
Sequence domains: ATP synthase
Structure domains:
ATP synthase subunit delta, mitochondrial Chain: H
Molecule details ›
Chain: H
Length: 138 amino acids
Theoretical weight: 14.57 KDa
Source organism: Saccharomyces cerevisiae S288C
UniProt:
  • Canonical: Q12165 (Residues: 23-160; Coverage: 86%)
Gene names: ATP16, D2935, YD8119.03, YDL004W
Sequence domains:
ATP synthase subunit epsilon, mitochondrial Chain: I
Molecule details ›
Chain: I
Length: 61 amino acids
Theoretical weight: 6.62 KDa
Source organism: Saccharomyces cerevisiae S288C
UniProt:
  • Canonical: P21306 (Residues: 2-62; Coverage: 98%)
Gene names: ATP15, P0345, YPL271W
Sequence domains: Mitochondrial ATP synthase epsilon chain
Structure domains: ATP synthase, F1 complex, epsilon subunit superfamily, mitochondrial
ATP synthase subunit 4, mitochondrial Chain: Z
Molecule details ›
Chain: Z
Length: 209 amino acids
Theoretical weight: 23.19 KDa
Source organism: Saccharomyces cerevisiae S288C
UniProt:
  • Canonical: P05626 (Residues: 36-244; Coverage: 86%)
Gene names: ATP4, LPF7C, YPL078C
Sequence domains: Mitochondrial ATP synthase B chain precursor (ATP-synt_B)
ATP synthase subunit d, mitochondrial Chain: 7
Molecule details ›
Chain: 7
Length: 173 amino acids
Theoretical weight: 19.71 KDa
Source organism: Saccharomyces cerevisiae S288C
UniProt:
  • Canonical: P30902 (Residues: 2-174; Coverage: 99%)
Gene names: ATP7, YKL016C
Sequence domains: ATP synthase D chain, mitochondrial (ATP5H)
ATP synthase subunit H, mitochondrial Chain: 6
Molecule details ›
Chain: 6
Length: 92 amino acids
Theoretical weight: 10.42 KDa
Source organism: Saccharomyces cerevisiae S288C
UniProt:
  • Canonical: Q12349 (Residues: 33-124; Coverage: 74%)
Gene names: ATP14, L8003.20, YLR295C
Sequence domains: ATP synthase complex subunit h
ATP synthase subunit f, mitochondrial Chain: U
Molecule details ›
Chain: U
Length: 95 amino acids
Theoretical weight: 10.58 KDa
Source organism: Saccharomyces cerevisiae S288C
UniProt:
  • Canonical: Q06405 (Residues: 7-101; Coverage: 94%)
Gene names: ATP17, D9481.21, YDR377W
Sequence domains: Mitochondrial F1-F0 ATP synthase subunit F of fungi
ATP synthase protein 8 Chain: 8
Molecule details ›
Chain: 8
Length: 48 amino acids
Theoretical weight: 5.83 KDa
Source organism: Saccharomyces cerevisiae S288C
UniProt:
  • Canonical: P00856 (Residues: 1-48; Coverage: 100%)
Gene names: AAP1, ATP8, Q0080
Sequence domains: Fungal ATP synthase protein 8 (A6L)
ATP synthase subunit a Chain: X
Molecule details ›
Chain: X
Length: 249 amino acids
Theoretical weight: 27.9 KDa
Source organism: Saccharomyces cerevisiae S288C
UniProt:
  • Canonical: P00854 (Residues: 11-259; Coverage: 96%)
Gene names: ATP6, OLI2, OLI4, PHO1, Q0085
Sequence domains: ATP synthase A chain
ATP synthase subunit J, mitochondrial Chain: J
Molecule details ›
Chain: J
Length: 37 amino acids
Theoretical weight: 4.15 KDa
Source organism: Saccharomyces cerevisiae S288C
UniProt:
  • Canonical: P81450 (Residues: 1-37; Coverage: 63%)
Gene names: ATP18, YML081BC, YML081C-A
Sequence domains: ATP synthase j chain

Ligands and Environments

2 bound ligands:
Ligand ATP 3 x ATP
Ligand ADP 2 x ADP
1 modified residue:
Ligand FME 10 x FME

Experiments and Validation Details

Entry percentile scores
Resolution: 3.6Å
Relevant EMDB volumes: EMD-7548

Quick links

Citations

29 review citations

The mitochondrial permeability transition: Recent progress and open questions.
Bernardi et al. (2022)
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14 mentions without citation

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Xu et al. (2020)
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