1nbm
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THE STRUCTURE OF BOVINE F1-ATPASE COVALENTLY INHIBITED WITH 4-CHLORO-7-NITROBENZOFURAZAN
OverviewOverview
BACKGROUND: F1-ATPase is the globular domain of F1F0-ATP synthase that, catalyses the hydrolysis of ATP to ADP and phosphate. The crystal, structure of bovine F1-ATPase has been determined previously to 2.8 A, resolution. The enzyme comprises five different subunits in the, stoichiometry alpha 3 beta 3 gamma delta epsilon; the three catalytic beta, subunits alternate with the three alpha subunits around the centrally, located single gamma subunit. To understand more about the catalytic, mechanisms, F1-ATPase was inhibited by reaction with, 4-chloro-7-nitrobenzofurazan (NBD-Cl) and the structure of the inhibited, complex (F1-NBD) determined by X-ray crystallography. RESULTS: In the, structure the three beta subunits adopt a different conformation with, different nucleotide occupancy. ... [(full description)]
About this StructureAbout this Structure
1NBM is a [Protein complex] structure of sequences from [Bos taurus] with MG, PO4, ATP and ADP as [ligands]. Active as [Transferred entry: 3.6.3.14], with EC number [3.6.1.34]. Structure known Active Sites: CA1, CA2, CA3, PL1, PL2, PL3, PL4, PL5, PL6 and PL7. Full crystallographic information is available from [OCA].
ReferenceReference
Bovine F1-ATPase covalently inhibited with 4-chloro-7-nitrobenzofurazan: the structure provides further support for a rotary catalytic mechanism., Orriss GL, Leslie AG, Braig K, Walker JE, Structure. 1998 Jul 15;6(7):831-7. PMID:9687365
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