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3.A.2.1.3
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:P09457
Protein Name:ATP5 aka ATPO aka OSCP aka YDR298C aka D9740.11
Length:212
Molecular Weight:22814.00
Species:Saccharomyces cerevisiae (Baker's yeast) [4932]
Location1 / Topology2 / Orientation3: Mitochondrion1
Substrate hydron

Cross database links:

DIP: DIP-3037N
RefSeq: NP_010584.1   
Entrez Gene ID: 851892   
Pfam: PF00213   
KEGG: sce:YDR298C   

Gene Ontology

GO:0000274 C:mitochondrial proton-transporting ATP synth...
GO:0005886 C:plasma membrane
GO:0045261 C:proton-transporting ATP synthase complex, c...
GO:0046933 F:hydrogen ion transporting ATP synthase acti...
GO:0015986 P:ATP synthesis coupled proton transport

References (6)

[1] “The sequence of the yeast ATP5 gene.”  Lee M.et.al.   2971156
[2] “The gene coding for the yeast oligomycin sensitivity-conferring protein.”  Uh M.et.al.   2146269
[3] “The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.”  Jacq C.et.al.   9169867
[4] “Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.”  Hu Y.et.al.   17322287
[5] “Global analysis of protein expression in yeast.”  Ghaemmaghami S.et.al.   14562106
[6] “Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase.”  Reinders J.et.al.   17761666
Structure:
6B8H   6CP3   6CP6     

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FASTA formatted sequence
1:	MFNRVFTRSF ASSLRAAASK AAAPPPVRLF GVEGTYATAL YQAAAKNSSI DAAFQSLQKV 
61:	ESTVKKNPKL GHLLLNPALS LKDRNSVIDA IVETHKNLDG YVVNLLKVLS ENNRLGCFEK 
121:	IASDFGVLND AHNGLLKGTV TSAEPLDPKS FKRIEKALSA SKLVGQGKSL KLENVVKPEI 
181:	KGGLIVELGD KTVDLSISTK IQKLNKVLED SI