1koj
From Proteopedia
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Crystal structure of rabbit phosphoglucose isomerase complexed with 5-phospho-D-arabinonohydroxamic acid
Overview
Phosphoglucose isomerase (EC ) catalyzes the second step in glycolysis, the reversible isomerization of D-glucose 6-phosphate to D-fructose, 6-phosphate. The reaction mechanism involves acid-base catalysis with, proton transfer and proceeds through a cis-enediol(ate) intermediate., 5-Phospho-D-arabinonohydroxamic acid (5PAH) is a synthetic small molecule, that resembles the reaction intermediate, differing only in that it has a, nitrogen atom in place of C1. Hence, 5PAH is the best inhibitor of the, isomerization reaction reported to date with a K(i) of 2 x 10(-7) M. Here, we report the crystal structure of rabbit phosphoglucose isomerase, complexed with 5PAH at 1.9 A resolution. The interaction of 5PAH with, amino acid residues in the enzyme active site supports a model of the, catalytic mechanism in which Glu-357 transfers a proton between C1 and C2, and Arg-272 helps stabilize the intermediate. It also suggests a mechanism, for proton transfer between O1 and O2.
About this Structure
1KOJ is a Single protein structure of sequence from Oryctolagus cuniculus with PAN as ligand. Active as Glucose-6-phosphate isomerase, with EC number 5.3.1.9 Full crystallographic information is available from OCA.
Reference
The crystal structure of rabbit phosphoglucose isomerase complexed with 5-phospho-D-arabinonohydroxamic acid., Arsenieva D, Hardre R, Salmon L, Jeffery CJ, Proc Natl Acad Sci U S A. 2002 Apr 30;99(9):5872-7. PMID:11983887
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