1KOJ

Crystal structure of rabbit phosphoglucose isomerase complexed with 5-phospho-D-arabinonohydroxamic acid

Summary for 1KOJ

• Entry DOI: 10.2210/pdb1koj/pdb
• Related: 1DQR 1G98 1HM5 1HOX 1IAT
• Descriptor: Glucose-6-phosphate isomerase, 5-PHOSPHO-D-ARABINOHYDROXAMIC ACID (3 entities in total)
• Functional Keywords: protein - inhibitor complex, isomerase
• Biological source: Oryctolagus cuniculus (rabbit)
• Cellular location: Cytoplasm: Q9N1E2
• Total number of polymer chains: 2
• Total formula weight: 125915.08

Authors

Arsenieva, D.,Hardre, R.,Salmon, L.,Jeffery, C.J. (deposition date: 2001-12-20, release date: 2002-05-03, Last modification date: 2023-08-16)

Primary citation

Arsenieva, D.,Hardre, R.,Salmon, L.,Jeffery, C.J.
The crystal structure of rabbit phosphoglucose isomerase complexed with 5-phospho-D-arabinonohydroxamic acid.
Proc.Natl.Acad.Sci.USA, 99:5872-5877, 2002

PubMed Abstract: 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.

PubMed: 11983887
DOI: 10.1073/pnas.052131799

Experimental method

X-RAY DIFFRACTION (1.9 Å)