1H8E

(ADP.AlF4)2(ADP.SO4) bovine F1-ATPase (all three catalytic sites occupied)

Summary for 1H8E

• Entry DOI: 10.2210/pdb1h8e/pdb
• Related: 1BMF 1COW 1E1Q 1E1R 1E79 1EFR 1H8H 1NBM 1QO1
• Descriptor: BOVINE MITOCHONDRIAL F1-ATPASE, SULFATE ION, ADENOSINE-5'-DIPHOSPHATE, ... (11 entities in total)
• Functional Keywords: hydrolase, atp phosphorylase, atp phosphorylase (h+ transporting), atp synthase, f1fo atp synthase, f1-atpase
• Biological source: BOS TAURUS (BOVINE); More
• Cellular location: Mitochondrion inner membrane (By similarity): P19483; Mitochondrion: P00829 P05631 P05630 P05632
• Total number of polymer chains: 9
• Total formula weight: 375479.73

Authors

Menz, R.I.,Walker, J.E.,Leslie, A.G.W. (deposition date: 2001-02-02, release date: 2001-08-10, Last modification date: 2023-12-13)

Primary citation

Menz, R.I.,Walker, J.E.,Leslie, A.G.W.
Structure of Bovine Mitochondrial F1-ATPase with Nucleotide Bound to All Three Catalytic Sites: Implications for the Mechanism of Rotary Catalysis
Cell(Cambridge,Mass.), 106:331-, 2001

PubMed Abstract: The crystal structure of a novel aluminium fluoride inhibited form of bovine mitochondrial F(1)-ATPase has been determined at 2 A resolution. In contrast to all previously determined structures of the bovine enzyme, all three catalytic sites are occupied by nucleotide. The subunit that did not bind nucleotide in previous structures binds ADP and sulfate (mimicking phosphate), and adopts a "half-closed" conformation. This structure probably represents the posthydrolysis, pre-product release step on the catalytic pathway. A catalytic scheme for hydrolysis (and synthesis) at physiological rates and a mechanism for the ATP-driven rotation of the gamma subunit are proposed based on the crystal structures of the bovine enzyme.

PubMed: 11509182
DOI: 10.1016/S0092-8674(01)00452-4

Experimental method

X-RAY DIFFRACTION (2 Å)