1G98

CRYSTAL STRUCTURE ANALYSIS OF RABBIT PHOSPHOGLUCOSE ISOMERASE COMPLEXED WITH 5-PHOSPHOARABINONATE, A TRANSITION STATE ANALOGUE

Summary for 1G98

• Entry DOI: 10.2210/pdb1g98/pdb
• Related: 1DQR
• Descriptor: PHOSPHOGLUCOSE ISOMERASE, 5-PHOSPHOARABINONIC ACID (3 entities in total)
• Functional Keywords: phosphoglucose isomerase, 5-phosphoarabinonate, transition state analogue, isomerase
• Biological source: Oryctolagus cuniculus (rabbit)
• Cellular location: Cytoplasm: Q9N1E2
• Total number of polymer chains: 2
• Total formula weight: 126147.46

Authors

Jeffery, C.J.,Hardre, R.,Salmon, L. (deposition date: 2000-11-22, release date: 2001-06-01, Last modification date: 2023-08-09)

Primary citation

Jeffery, C.J.,Hardre, R.,Salmon, L.
Crystal structure of rabbit phosphoglucose isomerase complexed with 5-phospho-D-arabinonate identifies the role of Glu357 in catalysis.
Biochemistry, 40:1560-1566, 2001

PubMed Abstract: 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.

PubMed: 11327814
DOI: 10.1021/bi0018483

Experimental method

X-RAY DIFFRACTION (1.9 Å)