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1g98
From Proteopedia
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CRYSTAL STRUCTURE ANALYSIS OF RABBIT PHOSPHOGLUCOSE ISOMERASE COMPLEXED WITH 5-PHOSPHOARABINONATE, A TRANSITION STATE ANALOGUE
Overview
Phosphoglucose isomerase (PGI; E.C. 5.3.1.9) catalyzes the second step in, glycolysis, the interconversion of D-glucose-6-phosphate and, D-fructose-6-phosphate. We determined the X-ray crystal structure of, rabbit PGI complexed with a competitive inhibitor of isomerase activity, 5-phospho-D-arabinonate (5PAA), at 1.9 A resolution. 5PAA is a better, mimic of the proposed cis-enediol(ate) intermediate than, 6-phospho-D-gluconate, which was used in a previously reported crystal, structure of rabbit PGI. The orientation of 5PAA bound in the enzyme, active site predicts that active site residue Glu357 is the residue that, transfers a proton between C2 and C1 of the proposed cis-enediol(ate), intermediate. Amino acid residues Arg272 and Lys210 are predicted to be, involved in stabilizing the negative charge of the intermediate.
About this Structure
1G98 is a Single protein structure of sequence from Oryctolagus cuniculus with PA5 as ligand. Active as Glucose-6-phosphate isomerase, with EC number 5.3.1.9 Full crystallographic information is available from OCA.
Reference
Crystal structure of rabbit phosphoglucose isomerase complexed with 5-phospho-D-arabinonate identifies the role of Glu357 in catalysis., Jeffery CJ, Hardre R, Salmon L, Biochemistry. 2001 Feb 13;40(6):1560-6. PMID:11327814
Page seeded by OCA on Tue Nov 20 15:50:31 2007
