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

Christopher Davies, Hilary Muirhead, John Chirgwin

Research output: Contribution to journalArticle

27 Citations (Scopus)

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

Fingerprint

Glucose-6-Phosphate Isomerase
carbohydrate metabolism
phosphates
analogs
Isomerases
Glucose-6-Phosphate
Carbohydrate Metabolism
glucose
inhibitors
enzymes
Crystal structure
Cytokines
proteins
catalysts
Catalysts
crystal structure
Enzymes
cells
Proteins
arabinonate-5-phosphate

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics
  • Condensed Matter Physics
  • Structural Biology

Cite this

The structure of human phosphoglucose isomerase complexed with a transition-state analogue. / Davies, Christopher; Muirhead, Hilary; Chirgwin, John.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 59, No. 6, 01.06.2003, p. 1111-1113.

Research output: Contribution to journalArticle

@article{6e5ebbdfd4974930a3e5c30e7787c424,
title = "The structure of human phosphoglucose isomerase complexed with a transition-state analogue",
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 {\AA} resolution. The structure helps to confirm the assignment of Glu357 as the base catalyst in the isomerase reaction.",
author = "Christopher Davies and Hilary Muirhead and John Chirgwin",
year = "2003",
month = "6",
day = "1",
doi = "10.1107/S0907444903007352",
language = "English (US)",
volume = "59",
pages = "1111--1113",
journal = "Acta Crystallographica Section D: Structural Biology",
issn = "0907-4449",
publisher = "John Wiley and Sons Inc.",
number = "6",

}

TY - JOUR

T1 - The structure of human phosphoglucose isomerase complexed with a transition-state analogue

AU - Davies, Christopher

AU - Muirhead, Hilary

AU - Chirgwin, John

PY - 2003/6/1

Y1 - 2003/6/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0038383074&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0038383074&partnerID=8YFLogxK

U2 - 10.1107/S0907444903007352

DO - 10.1107/S0907444903007352

M3 - Article

C2 - 12777791

AN - SCOPUS:0038383074

VL - 59

SP - 1111

EP - 1113

JO - Acta Crystallographica Section D: Structural Biology

JF - Acta Crystallographica Section D: Structural Biology

SN - 0907-4449

IS - 6

ER -