1gky
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(New page: 200px<br /><applet load="1gky" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gky, resolution 2.0Å" /> '''REFINED STRUCTURE OF ...)
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Revision as of 14:00, 20 November 2007
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REFINED STRUCTURE OF THE COMPLEX BETWEEN GUANYLATE KINASE AND ITS SUBSTRATE GMP AT 2.0 ANGSTROMS RESOLUTION
Overview
The crystal structure of guanylate kinase from Saccharomyces cerevisiae, complexed with its substrate GMP has been refined at a resolution of 2.0, A. The final crystallographic R-factor is 17.3% in the resolution range, 7.0 A to 2.0 A for all reflections of the 100% complete data set. The, final model has standard geometry with root-mean-square deviations of, 0.016 A in bond lengths and 3.0 in bond angles. It consists of all 186, amino acid residues, the N-terminal acetyl group, the substrate GMP, one, sulfate ion and 174 water molecules. Guanylate kinase is structurally, related to adenylate kinases and G-proteins with respect to its central, beta-sheet with connecting helices and the giant anion hole that binds, nucleoside triphosphates. These nucleotides are ATP and GTP for the, kinases and GTP for the G-proteins. The chain segment binding the, substrate GMP of guanylate kinase differs grossly from the respective part, of the adenylate kinases; it has no counterpart in the G-proteins. The, binding mode of GMP is described in detail. Probably, the observed, structure represents one of several structurally quite different, intermediate states of the catalytic cycle.
About this Structure
1GKY is a Single protein structure of sequence from Saccharomyces cerevisiae with SO4, ACE and 5GP as ligands. Active as Guanylate kinase, with EC number 2.7.4.8 Full crystallographic information is available from OCA.
Reference
Refined structure of the complex between guanylate kinase and its substrate GMP at 2.0 A resolution., Stehle T, Schulz GE, J Mol Biol. 1992 Apr 20;224(4):1127-41. PMID:1314905
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