title: Structure of a phosphoglycerate mutase:3-phosphoglyceric acid complex at 1.7 A.
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.
authors.affiliation: Schools of Chemistry, University of Exeter, Stocker Road, Exeter, Devon EX4 4QD, England.
authors.forename: G S
authors.initials: GS
authors.lastname: Crowhurst
authors.forename: A R
authors.initials: AR
authors.lastname: Dalby
authors.forename: M N
authors.initials: MN
authors.lastname: Isupov
authors.forename: J W
authors.initials: JW
authors.lastname: Campbell
authors.forename: J A
authors.initials: JA
authors.lastname: Littlechild
mesh_terms: D001665:Binding Sites; D018360:Crystallography, X-Ray; D005656:Fungal Proteins / Q000737:chemistry; D005988:Glyceric Acids / Q000737:chemistry*; D006860:Hydrogen Bonding; D008958:Models, Molecular; D010736:Phosphoglycerate Mutase / Q000737:chemistry*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013431:Sulfates / Q000737:chemistry
chemical_list: D005656:Fungal Proteins; D005988:Glyceric Acids; D013431:Sulfates; C005156:3-phosphoglycerate; D010736:Phosphoglycerate Mutase