1nbm
From Proteopedia
|
THE STRUCTURE OF BOVINE F1-ATPASE COVALENTLY INHIBITED WITH 4-CHLORO-7-NITROBENZOFURAZAN
Overview
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 Structure
1NBM is a [Protein complex] structure of sequences from [Bos taurus] with MG, PO4, ATP and ADP as [ligands]. Active as [Hydrolase], 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].
Reference
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
Page seeded by OCA on Tue Oct 30 08:32:39 2007
Categories: Bos taurus | Protein complex | Braig, K. | Leslie, A.G.W. | Orriss, G.L. | Walker, J.E. | ADP | ATP | MG | PO4 | 4-chloro-7-nitrobenzofurazan | Atp synthase | F1-atpase | F1fo atp synthase | Inhibition
