2cly
SUBCOMPLEX OF THE STATOR OF BOVINE MITOCHONDRIAL ATP SYNTHASE
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OverviewOverview
The structure of most of the peripheral stalk, or stator, of the F-ATPase from bovine mitochondria, determined at 2.8 A resolution, contains residues 79-183, 3-123 and 5-70 of subunits b, d and F6, respectively. It consists of a continuous curved alpha-helix about 160 A long in the single b-subunit, augmented by the predominantly alpha-helical d- and F6-subunits. The structure occupies most of the peripheral stalk in a low-resolution structure of the F-ATPase. The long helix in subunit b extends from near to the top of the F1 domain to the surface of the membrane domain, and it probably continues unbroken across the membrane. Its uppermost region interacts with the oligomycin sensitivity conferral protein, bound to the N-terminal region of one alpha-subunit in the F1 domain. Various features suggest that the peripheral stalk is probably rigid rather than resembling a flexible rope. It remains unclear whether the transient storage of energy required by the rotary mechanism takes place in the central stalk or in the peripheral stalk or in both domains.
About this StructureAbout this Structure
2CLY is a Protein complex structure of sequences from Bos taurus. Active as H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 Full crystallographic information is available from OCA.
ReferenceReference
On the structure of the stator of the mitochondrial ATP synthase., Dickson VK, Silvester JA, Fearnley IM, Leslie AG, Walker JE, EMBO J. 2006 Jun 21;25(12):2911-8. Epub 2006 Jun 8. PMID:16791136
Page seeded by OCA on Thu Feb 21 16:50:00 2008