BOVINE MITOCHONDRIAL F1-ATPASE INHIBITED BY MG2+ADP AND ALUMINIUM FLUORIDE

File:1e1r.gif


1e1r, resolution 2.5Å

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OverviewOverview

BACKGROUND: 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 ... [(full description)]

About this StructureAbout this Structure

1E1R is a [Protein complex] structure of sequences from [Bos taurus] with MG, PO4, ANP, ADP and AF3 as [ligands]. Active as [Transferred entry: 3.6.3.14], with EC number [3.6.1.34]. Structure known Active Sites: CAT and PLP. Full crystallographic information is available from [OCA].

ReferenceReference

Structure of bovine mitochondrial F(1)-ATPase inhibited by Mg(2+) ADP and aluminium fluoride., Braig K, Menz RI, Montgomery MG, Leslie AG, Walker JE, Structure. 2000 Jun 15;8(6):567-73. PMID:10873854

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