2jj2
From Proteopedia
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THE STRUCTURE OF F1-ATPASE INHIBITED BY QUERCETIN.
Overview
The structures of F(1)-ATPase from bovine heart mitochondria inhibited, with the dietary phytopolyphenol, resveratrol, and with the related, polyphenols quercetin and piceatannol have been determined at 2.3-, 2.4-, and 2.7-A resolution, respectively. The inhibitors bind to a common site, in the inside surface of an annulus made from loops in the three alpha-, and three beta-subunits beneath the "crown" of beta-strands in their, N-terminal domains. This region of F(1)-ATPase forms a bearing to allow, the rotation of the tip of the gamma-subunit inside the annulus during, catalysis. The binding site is a hydrophobic pocket between the C-terminal, tip of the gamma-subunit and the beta(TP) subunit, and the inhibitors are, bound via H-bonds mostly to their hydroxyl moieties mediated by bound, ... [(full description)]
About this Structure
2JJ2 is a [Protein complex] structure of sequences from [Bos taurus] with MG, AZI, PO4, ANP, ADP, QUE and GOL as [ligands]. Active as [[1]], with EC number [3.6.1.34]. Full crystallographic information is available from [OCA].
Reference
Mechanism of inhibition of bovine F1-ATPase by resveratrol and related polyphenols., Gledhill JR, Montgomery MG, Leslie AG, Walker JE, Proc Natl Acad Sci U S A. 2007 Aug 21;104(34):13632-7. Epub 2007 Aug 13. PMID:17698806
Page seeded by OCA on Mon Oct 29 19:02:37 2007
Categories: Bos taurus | Protein complex | Gledhill, J.R. | Leslie, A.G.W. | Montgomery, M.G. | Walker, J.E. | ADP | ANP | AZI | GOL | MG | PO4 | QUE | Acetylation | Alternative splicing | Atp synthesis | Atp-binding | Bovine | Cf(1) | F1-atpase | Hydrogen ion transport | Hydrolase | Hydrolysis | Ion transport | Mitochondrial | Mitochondrion | Nucleotide-binding | Pyrrolidone carboxylic acid | Quercetin | Transit peptide | Transport
