Structure of ATP synthase, the F 0 proton channel and rotating stalk are shown in blue, the F 1 synthase domain in red and the membrane in grey.
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, IPR001469).
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 delta subunit of ATP synthase is coded by gene ATP5O.
References
- ^ 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.
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. PubMed
This article includes text from the public domain Pfam and InterPro IPR000711
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