The structure of human phosphoglucose isomerase complexed with a transition-state analogue

Christopher Davies, Hilary Muirhead, John Chirgwin

Research output: Contribution to journalArticlepeer-review

29 Scopus citations

Abstract

Phosphoglucose isomerase (PGI) is a workhorse enzyme of carbohydrate metabolism that interconverts glucose 6-phosphate and fructose 6-phosphate. Outside the cell, however, the protein appears to function as a cytokine. A crystal structure of human PGI bound with 5-phosphoarabinonate, a strong inhibitor that mimics the cis-enediol(ate) intermediate of the reaction, has been determined at 2.5 Å resolution. The structure helps to confirm the assignment of Glu357 as the base catalyst in the isomerase reaction.

Original languageEnglish (US)
Pages (from-to)1111-1113
Number of pages3
JournalActa Crystallographica - Section D Biological Crystallography
Volume59
Issue number6
DOIs
StatePublished - Jun 1 2003
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology

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