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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:P38077
Protein Name:ATP3 aka ATPG aka YBR039W aka YBR0408
Length:311
Molecular Weight:34351.00
Species:Saccharomyces cerevisiae (Baker's yeast) [4932]
Location1 / Topology2 / Orientation3: Mitochondrion1 / Peripheral membrane protein2
Substrate hydron

Cross database links:

DIP: DIP-3035N
RefSeq: NP_009595.1   
Entrez Gene ID: 852327   
Pfam: PF00231   
KEGG: sce:YBR039W   

Gene Ontology

GO:0005756 C:mitochondrial proton-transporting ATP synth...
GO:0046933 F:hydrogen ion transporting ATP synthase acti...
GO:0005515 F:protein binding
GO:0046961 F:proton-transporting ATPase activity, rotati...
GO:0015986 P:ATP synthesis coupled proton transport

References (9)

[1] “Cloning of the yeast ATP3 gene coding for the gamma-subunit of F1 and characterization of atp3 mutants.”  Paul M.-F.et.al.   7929329
[2] “Mutations in the mitochondrial ATP synthase gamma subunit suppress a slow-growth phenotype of yme1 yeast lacking mitochondrial DNA.”  Weber E.R.et.al.   7498726
[3] “Studies on the ATP3 gene of Saccharomyces cerevisiae: presence of two closely linked copies, ATP3a and ATP3b, on the right arm of chromosome II.”  Ohnishi K.et.al.   12898710
[4] “Complete DNA sequence of yeast chromosome II.”  Feldmann H.et.al.   7813418
[5] “Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.”  Hu Y.et.al.   17322287
[6] “Global analysis of protein expression in yeast.”  Ghaemmaghami S.et.al.   14562106
[7] “Molecular architecture of the rotary motor in ATP synthase.”  Stock D.et.al.   10576729
[8] “Novel features of the rotary catalytic mechanism revealed in the structure of yeast F1 ATPase.”  Kabaleeswaran V.et.al.   17082766
[9] “Asymmetric structure of the yeast F1 ATPase in the absence of bound nucleotides.”  Kabaleeswaran V.et.al.   19233840
Structure:
2HLD   3FKS   2WPD   2XOK   3OE7   3OEE   3OEH   3OFN   3ZIA   3ZRY   [...more]

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MLSRIVSNNA TRSVMCHQAQ VGILYKTNPV RTYATLKEVE MRLKSIKNIE KITKTMKIVA 
61:	STRLSKAEKA KISAKKMDEA EQLFYKNAET KNLDVEATET GAPKELIVAI TSDKGLCGSI 
121:	HSQLAKAVRR HLNDQPNADI VTIGDKIKMQ LLRTHPNNIK LSINGIGKDA PTFQESALIA 
181:	DKLLSVMKAG TYPKISIFYN DPVSSLSFEP SEKPIFNAKT IEQSPSFGKF EIDTDANVPR 
241:	DLFEYTLANQ MLTAMAQGYA AEISARRNAM DNASKNAGDM INRYSILYNR TRQAVITNEL 
301:	VDIITGASSL G