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- Title
The structure of bovine F<sub>1</sub>-ATPase inhibited by ADP and beryllium fluoride.
- Authors
Kagawa, Reiko; Montgomery, Martin G.; Braig, Kerstin; Leslie, Andrew G.W.; Walker, John E.
- Abstract
The structure of bovine F1-ATPase inhibited with ADP and beryllium fluoride at 2.0 Å resolution contains two ADP.BeF3- complexes mimicking ATP, bound in the catalytic sites of the ßTP and ßDP subunits. Except for a 1 Å shift in the guanidinium of aArg373, the conformations of catalytic side chains are very similar in both sites. However, the ordered water molecule that carries out nucleophilic attack on the ?-phosphate of ATP during hydrolysis is 2.6 Å from the beryllium in the ßDP subunit and 3.8 Å away in the ßTP subunit, strongly indicating that the ßDP subunit is the catalytically active conformation. In the structure of F1-ATPase with five bound ADP molecules (three in a-subunits, one each in the ßTP and ßDP subunits), which has also been determined, the conformation of aArg373 suggests that it senses the presence (or absence) of the ?-phosphate of ATP. Two catalytic schemes are discussed concerning the various structures of bovine F1-ATPase.
- Subjects
CATTLE; ADENOSINE triphosphatase; ADENOSINE diphosphate; NUCLEOPHILIC reactions; HYDROLYSIS; CATALYSTS
- Publication
EMBO Journal, 2004, Vol 23, Issue 14, p2734
- ISSN
0261-4189
- Publication type
Article
- DOI
10.1038/sj.emboj.7600293