2v7q
From Proteopedia
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THE STRUCTURE OF F1-ATPASE INHIBITED BY I1-60HIS, A MONOMERIC FORM OF THE INHIBITOR PROTEIN, IF1.
Overview
The structure of bovine F(1)-ATPase inhibited by a monomeric form of the, inhibitor protein, IF(1), known as I1-60His, lacking most of the, dimerization region, has been determined at 2.1-A resolution. The resolved, region of the inhibitor from residues 8-50 consists of an extended, structure from residues 8-13, followed by two alpha-helices from residues, 14-18 and residues 21-50 linked by a turn. The binding site in the, beta(DP)-alpha(DP) catalytic interface is complex with contributions from, five different subunits of F(1)-ATPase. The longer helix extends from the, external surface of F(1) via a deep groove made from helices and loops in, the C-terminal domains of subunits beta(DP), alpha(DP), beta(TP), and, alpha(TP) to the internal cavity surrounding the central stalk. The linker, ... [(full description)]
About this Structure
2V7Q is a [Protein complex] structure of sequences from [Bos taurus] and [Bos taurus] with MG, PO4, ATP and ADP as [ligands]. Active as [[1]], with EC number [3.6.1.14]. Full crystallographic information is available from [OCA].
Reference
How the regulatory protein, IF1, inhibits F1-ATPase from bovine mitochondria., Gledhill JR, Montgomery MG, Leslie AG, Walker JE, Proc Natl Acad Sci U S A. 2007 Oct 2;104(40):15671-6. Epub 2007 Sep 25. PMID:17895376
Page seeded by OCA on Mon Oct 29 23:05:04 2007
Categories: Bos taurus | Protein complex | Gledhill, J.R. | Leslie, A.G.W. | Montgomery, M.G. | Walker, J.E. | ADP | ATP | MG | PO4 | Acetylation | Alternative splicing | Atp synthesis | Atp-binding | Bovine | Cf(1) | Coiled coil | F1-atpase | Hydrogen ion transport | Hydrolase | Hydrolysis | Inhibitor protein | Ion transport | Mitochondrial | Mitochondrion | Nucleotide-binding | Pyrrolidone carboxylic acid | Transit peptide | Transport
