2WSS

The structure of the membrane extrinsic region of bovine ATP synthase

Summary for 2WSS

• Entry DOI: 10.2210/pdb2wss/pdb
• Related: 1BMF 1COW 1E1Q 1E1R 1E79 1EFR 1H8E 1H8H 1NBM 1OHH 1QO1 1VZS 1W0J 1W0K 2BO5 2CK3 2CLY 2JDI 2JIZ 2JJ1 2JJ2 2V7Q 2W6E 2W6F 2W6G 2W6H 2W6I 2W6J
• Descriptor: ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MAGNESIUM ION, ... (12 entities in total)
• Functional Keywords: hydrogen ion transport, atp synthesis, phosphoprotein, ubl conjugation, transit peptide, nucleotide-binding, acetylation, atp-binding, ion transport, mitochondrion, pyrrolidone carboxylic acid, hydrolase, transport
• Biological source: BOS TAURUS (BOVINE); More
• Total number of polymer chains: 25
• Total formula weight: 851827.38

Authors

Rees, D.M.,Leslie, A.G.W.,Walker, J.E. (deposition date: 2009-09-09, release date: 2009-11-17, Last modification date: 2024-11-13)

Primary citation

Rees, D.M.,Leslie, A.G.W.,Walker, J.E.
The Structure of the Membrane Extrinsic Region of Bovine ATP Synthase
Proc.Natl.Acad.Sci.USA, 106:21597-, 2009

PubMed Abstract: The structure of the complex between bovine mitochondrial F(1)-ATPase and a stator subcomplex has been determined at a resolution of 3.2 A. The resolved region of the stator contains residues 122-207 of subunit b; residues 5-25 and 35-57 of F(6); 3 segments of subunit d from residues 30-40, 65-74, and 85-91; and residues 1-146 and 169-189 of the oligomycin sensitivity conferral protein (OSCP). The stator subcomplex represents its membrane distal part, and its structure has been augmented with an earlier structure of a subcomplex containing residues 79-183, 3-123, and 5-70 of subunits b, d, and F(6), respectively, which extends to the surface of the inner membrane of the mitochondrion. The N-terminal domain of the OSCP links the stator with F(1)-ATPase via alpha-helical interactions with the N-terminal region of subunit alpha(E). Its C-terminal domain makes extensive helix-helix interactions with the C-terminal alpha-helix of subunit b from residues 190-207. Subunit b extends as a continuous 160-A long alpha-helix from residue 188 back to residue 79 near to the surface of the inner mitochondrial membrane. This helix appears to be stiffened by other alpha-helices in subunits d and F(6), but the structure can bend inward toward the F(1) domain around residue 146 of subunit b. The linker region between the 2 domains of the OSCP also appears to be flexible, enabling the stator to adjust its shape as it passes over the changing profile of the F(1) domain during a catalytic cycle. The structure of the membrane extrinsic part of bovine ATP synthase is now complete.

PubMed: 19995987
DOI: 10.1073/PNAS.0910365106

Experimental method

X-RAY DIFFRACTION (3.2 Å)