Nature. 1994 Aug 25;370(6491):621-8.

Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria.

Abrahams JP, Leslie AG, Lutter R, Walker JE.

Source

Medical Research Council Laboratory of Molecular Biology, Cambridge, UK.

Abstract

In the crystal structure of bovine mitochondrial F1-ATPase determined at 2.8 A resolution, the three catalytic beta-subunits differ in conformation and in the bound nucleotide. The structure supports a catalytic mechanism in intact ATP synthase in which the three catalytic subunits are in different states of the catalytic cycle at any instant. Interconversion of the states may be achieved by rotation of the alpha 3 beta 3 subassembly relative to an alpha-helical domain of the gamma-subunit.

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Nature. 1994 Aug 25;370(6491):594-5.

PMID:: 8065448; [PubMed - indexed for MEDLINE]

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Cited by over 100 PubMed Central articles

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Structures reported by this article

Bovine Mitochondrial F1-Atpase Complexed With The Peptide Antibiotic Efrapeptin

PDB: 1EFR

Source: Bos taurus

Method: X-Ray Diffraction

Resolution: 3.1 Å

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