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|1koj, resolution 1.90Å ()|
|Related:||1dqr, 1hox, 1hm5, 1iat, 1g98|
Crystal structure of rabbit phosphoglucose isomerase complexed with 5-phospho-D-arabinonohydroxamic acid
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
- Arsenieva D, Hardre R, Salmon L, Jeffery CJ. The crystal structure of rabbit phosphoglucose isomerase complexed with 5-phospho-D-arabinonohydroxamic acid. Proc Natl Acad Sci U S A. 2002 Apr 30;99(9):5872-7. PMID:11983887 doi:10.1073/pnas.052131799
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