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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:P05626
Protein Name:ATP4 aka ATPF aka YPL078C aka LPF7C
Length:244
Molecular Weight:27010.00
Species:Saccharomyces cerevisiae (Baker's yeast) [4932]
Number of TMSs:2
Location1 / Topology2 / Orientation3: Mitochondrion1
Substrate hydron

Cross database links:

DIP: DIP-3036N
RefSeq: NP_015247.1   
Entrez Gene ID: 856027   
Pfam: PF05405   
KEGG: sce:YPL078C   

Gene Ontology

GO:0000276 C:mitochondrial proton-transporting ATP synth...
GO:0015078 F:hydrogen ion transmembrane transporter acti...
GO:0005515 F:protein binding
GO:0015986 P:ATP synthesis coupled proton transport

References (6)

[1] “ATP4, the structural gene for yeast F0F1 ATPase subunit 4.”  Velours J.et.al.   2892678
[2] “The yeast ATP synthase subunit 4: structure and function.”  Velours J.et.al.   2553130
[3] “The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.”  Bussey H.et.al.   9169875
[4] “Subunit 4 of ATP synthase (F0F1) from yeast mitochondria. Purification, amino-acid composition and partial N-terminal sequence.”  Velours J.et.al.   2883007
[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:
6B2Z   6B8H   6CP3   6CP5   6CP6   6CP7   6WTD     

External Searches:

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MSMSMGVRGL ALRSVSKTLF SQGVRCPSMV IGARYMSSTP EKQTDPKAKA NSIINAIPGN 
61:	NILTKTGVLG TSAAAVIYAI SNELYVINDE SILLLTFLGF TGLVAKYLAP AYKDFADARM 
121:	KKVSDVLNAS RNKHVEAVKD RIDSVSQLQN VAETTKVLFD VSKETVELES ERFELKQKVE 
181:	LAHEAKAVLD SWVRYEASLR QLEQRQLAKS VISRVQSELG NPKFQEKVLQ QSISEIEQLL 
241:	SKLK