2CLY

Subcomplex of the stator of bovine mitochondrial ATP synthase

Summary for 2CLY

• Entry DOI: 10.2210/pdb2cly/pdb
• Related: 1VZS
• Descriptor: ATP SYNTHASE B CHAIN, MITOCHONDRIAL, ATP SYNTHASE D CHAIN, MITOCHONDRIAL, ATP SYNTHASE COUPLING FACTOR 6, MITOCHONDRIAL, ... (4 entities in total)
• Functional Keywords: mitochondria, mitochondrion, ion transport, cf(0), stator, transport, acetylation, atp synthase, hydrogen ion transport, transit peptide, peripheral stalk, hydrolase
• Biological source: BOS TAURUS (BOVINE); More
• Cellular location: Mitochondrion: P13619 P13620 P02721
• Total number of polymer chains: 6
• Total formula weight: 104818.44

Authors

Kane Dickson, V.,Silvester, J.A.,Fearnley, I.M.,Leslie, A.G.W.,Walker, J.E. (deposition date: 2006-05-03, release date: 2006-06-28, Last modification date: 2024-05-08)

Primary citation

Kane Dickson, V.,Silvester, J.A.,Fearnley, I.M.,Leslie, A.G.W.,Walker, J.E.
On the Structure of the Stator of the Mitochondrial ATP Synthase.
Embo J., 25:2911-, 2006

PubMed Abstract: 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.

PubMed: 16791136
DOI: 10.1038/SJ.EMBOJ.7601177

Experimental method

X-RAY DIFFRACTION (2.8 Å)