Structure of a phosphoglycerate mutase:3-phosphoglyceric acid complex at 1.7 A

G S Crowhurst; A R Dalby; M N Isupov; J W Campbell; J A Littlechild

doi:10.1107/s0907444999009944

Structure of a phosphoglycerate mutase:3-phosphoglyceric acid complex at 1.7 A

Acta Crystallogr D Biol Crystallogr. 1999 Nov;55(Pt 11):1822-6. doi: 10.1107/s0907444999009944.

Authors

G S Crowhurst¹, A R Dalby, M N Isupov, J W Campbell, J A Littlechild

Affiliation

¹ Schools of Chemistry, University of Exeter, Stocker Road, Exeter, Devon EX4 4QD, England.

PMID: 10531478
DOI: 10.1107/s0907444999009944

Abstract

The crystal structure of the tetrameric glycolytic enzyme phosphoglycerate mutase from the yeast Saccharomyces cerevisiae has been determined to 1.7 A resolution in complex with the sugar substrate. The difference map indicates that 3-phosphoglycerate is bound at the base of a 12 A cleft, positioning C2 of the substrate within 3.5 A of the primary catalytic residue, histidine 8.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Binding Sites
Crystallography, X-Ray
Fungal Proteins / chemistry
Glyceric Acids / chemistry*
Hydrogen Bonding
Models, Molecular
Phosphoglycerate Mutase / chemistry*
Saccharomyces cerevisiae / enzymology*
Sulfates / chemistry

Substances

Fungal Proteins
Glyceric Acids
Sulfates
3-phosphoglycerate
Phosphoglycerate Mutase

Associated data

PDB/1QHF