1W0J
Beryllium fluoride inhibited bovine F1-ATPase
Summary for 1W0J
Entry DOI | 10.2210/pdb1w0j/pdb |
Related | 1BMF 1COW 1E1Q 1E1R 1E79 1EFR 1H8E 1H8H 1NBM 1OHH 1QO1 1W0K |
Descriptor | ATP SYNTHASE ALPHA CHAIN HEART ISOFORM, MITOCHONDRIAL PRECURSOR, ATP SYNTHASE BETA CHAIN, MITOCHONDRIAL PRECURSOR, ATP SYNTHASE GAMMA CHAIN, MITOCHONDRIAL PRECURSOR, ... (9 entities in total) |
Functional Keywords | atp phosphorylase, atp phosphorylase (h+ transporting), atp synthase, f1fo atp synthase, f1-atpase, hydrolase, atp synthesis, atp-binding |
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 | 354215.69 |
Authors | Kagawa, R.,Montgomery, M.G.,Braig, K.,Walker, J.E.,Leslie, A.G.W. (deposition date: 2004-06-08, release date: 2004-07-08, Last modification date: 2023-12-13) |
Primary citation | Kagawa, R.,Montgomery, M.G.,Braig, K.,Leslie, A.G.W.,Walker, J.E. The Structure of Bovine F1-ATPase Inhibited by Adp and Beryllium Fluoride Embo J., 23:2734-, 2004 Cited by PubMed Abstract: The structure of bovine F1-ATPase inhibited with ADP and beryllium fluoride at 2.0 angstroms resolution contains two ADP.BeF3- complexes mimicking ATP, bound in the catalytic sites of the beta(TP) and beta(DP) subunits. Except for a 1 angstrom shift in the guanidinium of alphaArg373, the conformations of catalytic side chains are very similar in both sites. However, the ordered water molecule that carries out nucleophilic attack on the gamma-phosphate of ATP during hydrolysis is 2.6 angstroms from the beryllium in the beta(DP) subunit and 3.8 angstroms away in the beta(TP) subunit, strongly indicating that the beta(DP) subunit is the catalytically active conformation. In the structure of F1-ATPase with five bound ADP molecules (three in alpha-subunits, one each in the beta(TP) and beta(DP) subunits), which has also been determined, the conformation of alphaArg373 suggests that it senses the presence (or absence) of the gamma-phosphate of ATP. Two catalytic schemes are discussed concerning the various structures of bovine F1-ATPase. PubMed: 15229653DOI: 10.1038/SJ.EMBOJ.7600293 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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