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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:P61829
Protein Name:ATP9 aka OLI1 aka OLI2 aka OLI3
Molecular Weight:7759.00
Species:Saccharomyces cerevisiae (Baker's yeast) [4932]
Number of TMSs:2
Location1 / Topology2 / Orientation3: Mitochondrion membrane1 / Multi-pass membrane protein2
Substrate hydron

Cross database links:

DIP: DIP-3041N
RefSeq: NP_009319.1   
Entrez Gene ID: 854584   
Pfam: PF00137   
KEGG: sce:Q0130   

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:0008289 F:lipid binding
GO:0015986 P:ATP synthesis coupled proton transport

References (6)

[1] “Nucleotide sequence of the mitochondrial structural gene for subunit 9 of yeast ATPase complex.”  Hensgens   156363
[2] “Assembly of the mitochondrial membrane system. The DNA sequence of a mitochondrial ATPase gene in Saccharomyces cerevisiae.”  Macino   155696
[3] “Biogenesis of mitochondria: DNA sequence analysis of mit- mutations in the mitochondrial oli1 gene coding for mitochondrial ATPase subunit 9 in Saccharomyces cerevisiae.”  Ooi   2860638
[4] “The complete sequence of the mitochondrial genome of Saccharomyces cerevisiae.”  Foury   9872396
[5] “NH2-terminal sequence of the isolated yeast ATP synthase subunit 6 reveals post-translational cleavage.”  Michon   2894987
[6] “Molecular architecture of the rotary motor in ATP synthase.”  Stock   10576729
2WPD   2XOK   3U2F   3U2Y   3U32   3UD0   3ZRY   4B2Q   4F4S   5BPS   [...more]

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