1E1Q

BOVINE MITOCHONDRIAL F1-ATPASE AT 100K

Summary for 1E1Q

• Entry DOI: 10.2210/pdb1e1q/pdb
• Related: 1BMF 1COW 1E1R 1EFR 1NBM 1QO1
• Descriptor: BOVINE MITOCHONDRIAL F1-ATPASE, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MAGNESIUM ION, ... (8 entities in total)
• Functional Keywords: 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
• Total number of polymer chains: 7
• Total formula weight: 354031.28

Authors

Braig, K.,Menz, R.I.,Montgomery, M.G.,Leslie, A.G.W.,Walker, J.E. (deposition date: 2000-05-10, release date: 2000-06-28, Last modification date: 2023-12-06)

Primary citation

Braig, K.,Menz, R.I.,Montgomery, M.G.,Leslie, A.G.W.,Walker, J.E.
Structure of Bovine Mitochondrial F1-ATPase Inhibited by Mg2+Adp and Aluminium Fluoride
Structure, 8:567-, 2000

PubMed Abstract: The globular domain of the membrane-associated F(1)F(o)-ATP synthase complex can be detached intact as a water-soluble fragment known as F(1)-ATPase. It consists of five different subunits, alpha, beta, gamma, delta and epsilon, assembled with the stoichiometry 3:3:1:1:1. In the crystal structure of bovine F(1)-ATPase determined previously at 2.8 A resolution, the three catalytic beta subunits and the three noncatalytic alpha subunits are arranged alternately around a central alpha-helical coiled coil in the gamma subunit. In the crystals, the catalytic sites have different nucleotide occupancies. One contains the triphosphate form of the nucleotide, the second contains the diphosphate, and the third is unoccupied. Fluoroaluminate complexes have been shown to mimic the transition state in several ATP and GTP hydrolases. In order to understand more about its catalytic mechanism, F(1)-ATPase was inhibited with Mg(2+)ADP and aluminium fluoride and the structure of the inhibited complex was determined by X-ray crystallography.

PubMed: 10873854
DOI: 10.1016/S0969-2126(00)00145-3

Experimental method

X-RAY DIFFRACTION (2.61 Å)