4ASU

F1-ATPase in which all three catalytic sites contain bound nucleotide, with magnesium ion released in the Empty site

Summary for 4ASU

• Entry DOI: 10.2210/pdb4asu/pdb
• Related: 1BMF 1COW 1E1Q 1E1R 1E79 1EFR 1H8E 1H8H 1NBM 1OHH 1QO1 1W0J 1W0K 2CK3 2JDI 2JIZ 2JJ1 2JJ2 2V7Q 2W6E 2W6F 2W6G 2W6H 2W6I 2W6J 2WSS 2XND
• Descriptor: ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL, ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL, ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL, ... (8 entities in total)
• Functional Keywords: hydrolase
• Biological source: BOS TAURUS (CATTLE); More
• Cellular location: Mitochondrion inner membrane (By similarity): P19483; Mitochondrion: P00829 P05631 P05630 P05632
• Total number of polymer chains: 9
• Total formula weight: 374473.67

Authors

Rees, D.M.,Montgomery, M.G.,Leslie, A.G.W.,Walker, J.E. (deposition date: 2012-05-03, release date: 2012-06-27, Last modification date: 2023-12-20)

Primary citation

Rees, D.M.,Montgomery, M.G.,Leslie, A.G.,Walker, J.E.
Structural Evidence of a New Catalytic Intermediate in the Pathway of ATP Hydrolysis by F1-ATPase from Bovine Heart Mitochondria.
Proc.Natl.Acad.Sci.USA, 109:11139-, 2012

PubMed Abstract: The molecular description of the mechanism of F(1)-ATPase is based mainly on high-resolution structures of the enzyme from mitochondria, coupled with direct observations of rotation in bacterial enzymes. During hydrolysis of ATP, the rotor turns counterclockwise (as viewed from the membrane domain of the intact enzyme) in 120° steps. Because the rotor is asymmetric, at any moment the three catalytic sites are at different points in the catalytic cycle. In a "ground-state" structure of the bovine enzyme, one site (β(E)) is devoid of nucleotide and represents a state that has released the products of ATP hydrolysis. A second site (β(TP)) has bound the substrate, magnesium. ATP, in a precatalytic state, and in the third site (β(DP)), the substrate is about to undergo hydrolysis. Three successive 120° turns of the rotor interconvert the sites through these three states, hydrolyzing three ATP molecules, releasing the products and leaving the enzyme with two bound nucleotides. A transition-state analog structure, F(1)-TS, displays intermediate states between those observed in the ground state. For example, in the β(DP)-site of F(1)-TS, the terminal phosphate of an ATP molecule is undergoing in-line nucleophilic attack by a water molecule. As described here, we have captured another intermediate in the catalytic cycle, which helps to define the order of substrate release. In this structure, the β(E)-site is occupied by the product ADP, but without a magnesium ion or phosphate, providing evidence that the nucleotide is the last of the products of ATP hydrolysis to be released.

PubMed: 22733764
DOI: 10.1073/PNAS.1207587109

Experimental method

X-RAY DIFFRACTION (2.6 Å)