2jj2 | pdb_00002jj2
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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
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- 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