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ATP synthase delta/OSCP subunit

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This is an old revision of this page, as edited by Hodja Nasreddin (talk | contribs) at 04:54, 25 December 2007 (Created page with '{{Pfam_box | Symbol = OSCP | Name = ATP synthase delta (OSCP) subunit | image = | width = | caption = | Pfam= PF00213 | InterPro= IPR000711 | SMART= | Prosite = PDO...'). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.
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ATP synthase delta (OSCP) subunit
Identifiers
SymbolOSCP
PfamPF00213
InterProIPR000711
PROSITEPDOC00327
SCOP21abv / SCOPe / SUPFAM
TCDB3.A.2
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB2a7uB:7-135 1abv :7-106 2bo5A:37-143

ATP synthase delta subunit is a subunit of bacterial and chloroplast ATPase, or OSCP (oligomycin sensitivity conferral protein) in mitochondrial ATPase (note that in mitochondria there is a different delta subunit, InterProIPR001469).

The OSCP/delta subunit appears to be part of the peripheral stalk that holds the F1 complex alpha3beta3 catalytic core stationary against the torque of the rotating central stalk, and links subunit A of the F0 complex with the F1 complex. In mitochondria, the peripheral stalk consists of OSCP, as well as F0 components F6, B and D. In bacteria and chloroplasts the peripheral stalks have different subunit compositions: delta and two copies of F0 component B (bacteria), or delta and F0 components B and B (chloroplasts)[1].

Human proteins containing this domain

ATP5O;

References

  1. ^ Walker JE, Runswick MJ, Neuhaus D, Montgomery MG, Carbajo RJ, Kellas FA (2005). "Structure of the F1-binding domain of the stator of bovine F1Fo-ATPaseand how it binds an alpha-subunit". J. Mol. Biol. 351 (4): 824–838. PMID 16045926.{{cite journal}}: CS1 maint: multiple names: authors list (link)

Further reading

  • [1]. Structure and arrangement of the delta subunit in the E. coli ATP synthase (ECF1F0). Wilkens S, Rodgers A, Ogilvie I, Capaldi RA; Biophys Chem 1997;68:95-102. PMID 9468613
This article incorporates text from the public domain Pfam and InterPro: IPR000711