1NBM

THE STRUCTURE OF BOVINE F1-ATPASE COVALENTLY INHIBITED WITH 4-CHLORO-7-NITROBENZOFURAZAN

Summary for 1NBM

• Entry DOI: 10.2210/pdb1nbm/pdb
• Descriptor: F1-ATPASE, MAGNESIUM ION, ADENOSINE-5'-TRIPHOSPHATE, ... (9 entities in total)
• Functional Keywords: atp synthase, f1fo atp synthase, f1-atpase, 4-chloro-7-nitrobenzofurazan, inhibition
• Biological source: Bos taurus (cattle); More
• Cellular location: Mitochondrion inner membrane (By similarity): P19483; Mitochondrion: P00829 P00829 P05631
• Total number of polymer chains: 7
• Total formula weight: 353494.68

Authors

Orriss, G.L.,Leslie, A.G.W.,Braig, K.,Walker, J.E. (deposition date: 1998-04-30, release date: 1998-08-26, Last modification date: 2024-04-03)

Primary citation

Orriss, G.L.,Leslie, A.G.,Braig, K.,Walker, J.E.
Bovine F1-ATPase covalently inhibited with 4-chloro-7-nitrobenzofurazan: the structure provides further support for a rotary catalytic mechanism.
Structure, 6:831-837, 1998

PubMed Abstract: 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.

PubMed: 9687365
DOI: 10.1016/S0969-2126(98)00085-9

Experimental method

X-RAY DIFFRACTION (3 Å)