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H+-translocating F-type ATPase. Evidence of the proximity of ATP synthase subunit 6 is in proximity to the membrane in the supramolecular form (Velours et al., 2011).  The structure of the intact monomeric ATP synthase from the fungus, Pichia angusta, has been solved by electron cryo-microscopy (Vinothkumar et al. 2016). The Mg2+ and Ca2+-dependent enzymes are both active, but exhibit quite different behaviors (Nesci et al. 2017). Dimerization is necessary to create the inner membrane folds (cristae) characteristic of mitochondria.  Using cryo-electron microscopy, Guo et al. 2017 determined the structure of the dimeric FO complex from Saccharomyces cerevisiae at a resolution of 3.6 angstroms. The structure clarifies how the protons travel through the complex, how the complex dimerizes, and how the dimers bend the membrane to produce cristae. The crystal structure of the c-subunit ring with bound oligomycin revealed the inhibitor docked on the outer face of the proton-binding sites, deep in the transmembrane region (Zhou and Faraldo-Gómez 2018). A high resolution (3.7 Å) structure of the entire monomeric ATPase has been solved by cryo EM, suggesting how it is inhibited by oligomycin (Srivastava et al. 2018).  Absence of the e and g subunits decreases conductance of the F-ATP synthase channel about tenfold. Ablation of the first TMS of subunit b, which creates a distinct lateral domain with e and g, further affected channel activity. Thus, F-ATP synthase e, g and b subunits create a domain within the membrane that is critical for the generation of the high-conductance channel that is a prime candidate for formation of the permeability transition pore (PTP). Subunits e and g are only present in eukaryotes and may have evolved to confer this novel function to F-ATP synthases (Carraro et al. 2018). The translation rate of all yeast mitochondrial mRNAs, including all F-type ATPase subunits has been studied (Chicherin et al. 2021). Attenuated ADP-inhibition of F0F1 ATPase mitigates manifestations of mitochondrial dysfunction in yeast (Lapashina et al. 2022).

Accession Number:P00856
Protein Name:ATP8 aka AAP1
Molecular Weight:5822.00
Species:Saccharomyces cerevisiae (Baker's yeast) [4932]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Mitochondrion membrane1 / Single-pass membrane protein2
Substrate hydron

Cross database links:

DIP: DIP-3040N
RefSeq: NP_009312.1   
Entrez Gene ID: 854600   
Pfam: PF05933   
KEGG: sce:Q0080   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0000276 C:mitochondrial proton-transporting ATP synth...
GO:0015078 F:hydrogen ion transmembrane transporter acti...
GO:0015986 P:ATP synthesis coupled proton transport

References (3)

[1] “Biogenesis of mitochondria: the mitochondrial gene (aap1) coding for mitochondrial ATPase subunit 8 in Saccharomyces cerevisiae.”  McReadie   6223276
[2] “Organization and processing of the mitochondrial oxi3/oli2 multigenic transcript in yeast.”  Simon   6387398
[3] “The complete sequence of the mitochondrial genome of Saccharomyces cerevisiae.”  Foury   9872396
6B2Z   6B8H   6CP3   6CP5   6CP6   6CP7   6WTD     

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