ATP synthase delta/OSCP subunit
| ATP synthase delta (OSCP) subunit | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
 Structure of the N-terminal domain of the delta subunit of the E. coli ATPsynthase.[1] | |||||||||||
| Identifiers | |||||||||||
| Symbol | OSCP | ||||||||||
| Pfam | PF00213 | ||||||||||
| InterPro | IPR000711 | ||||||||||
| PROSITE | PDOC00327 | ||||||||||
| SCOP2 | 1abv / SCOPe / SUPFAM | ||||||||||
| TCDB | 3.A.2 | ||||||||||
| |||||||||||
ATP synthase delta subunit is a subunit of bacterial and chloroplast F-ATPase/synthase. It is known as OSCP (oligomycin sensitivity conferral protein) in mitochondrial ATPase (note that in mitochondria there is a different delta subunit, ATP synthase delta/epsilon subunit).
The OSCP/delta subunit appears to be part of the peripheral stalk that holds the F1 complex α3β3 catalytic core stationary against the torque of the rotating central stalk, and links subunit A of the FO complex with the F1 complex. In mitochondria, the peripheral stalk consists of OSCP, as well as FO components F6, B and D. In bacteria and chloroplasts the peripheral stalks have different subunit compositions: delta and two copies of FO component B (bacteria), or delta and FO components B and B' (chloroplasts).[2]
F-ATPases lacking this subunit generally transport sodium instead of protons. They are proposed to be called N-ATPases, since they seem to form a distinct group that is further apart from usual F-ATPases than A-ATPases are from V-ATPases.[3]
Human delta subunit of ATP synthase is coded by gene ATP5O.
References
[edit]- ^ Wilkens S, Dunn SD, Chandler J, Dahlquist FW, Capaldi RA (March 1997). "Solution structure of the N-terminal domain of the delta subunit of the E. coli ATPsynthase". Nat. Struct. Biol. 4 (3): 198–201. doi:10.1038/nsb0397-198. PMID 9164460. S2CID 11261505.
- ^ 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. doi:10.1016/j.jmb.2005.06.012. PMID 16045926.
- ^ Dibrova, DV; Galperin, MY; Mulkidjanian, AY (15 June 2010). "Characterization of the N-ATPase, a distinct, laterally transferred Na+-translocating form of the bacterial F-type membrane ATPase". Bioinformatics. 26 (12): 1473–6. doi:10.1093/bioinformatics/btq234. PMC 2881411. PMID 20472544.
Further reading
[edit]Wilkens, S.; Rodgers, A.; Ogilvie, I.; Capaldi, R. A. (1997). "Structure and arrangement of the delta subunit in the E. Coli ATP synthase (ECF1F0)". Biophysical Chemistry. 68 (1–3): 95–102. doi:10.1016/s0301-4622(97)00018-5. PMID 9468613.
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