1BMF

BOVINE MITOCHONDRIAL F1-ATPASE

Summary for 1BMF

• Entry DOI: 10.2210/pdb1bmf/pdb
• Descriptor: BOVINE MITOCHONDRIAL F1-ATPASE, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (7 entities in total)
• Functional Keywords: atp phosphorylase (h+ transporting), atp synthase, f1fo atp synthase, f1-atpase, atp phosphorylase
• Biological source: Bos taurus (cattle); More
• Cellular location: Mitochondrion inner membrane (By similarity): P19483; Mitochondrion: P00829 P05631
• Total number of polymer chains: 7
• Total formula weight: 353936.31

Authors

Abrahams, J.P.,Leslie, A.G.W.,Lutter, R.,Walker, J.E. (deposition date: 1996-03-13, release date: 1996-12-07, Last modification date: 2024-04-03)

Primary citation

Abrahams, J.P.,Leslie, A.G.,Lutter, R.,Walker, J.E.
Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria.
Nature, 370:621-628, 1994

PubMed 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.

PubMed: 8065448
DOI: 10.1038/370621a0

Experimental method

X-RAY DIFFRACTION (2.85 Å)