Structure of a phosphoglycerate mutase:3-phosphoglyceric acid complex at 1.7 A.
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.
Crowhurst
G S
GS
Schools of Chemistry, University of Exeter, Stocker Road, Exeter, Devon EX4 4QD, England.
Dalby
A R
AR
Isupov
M N
MN
Campbell
J W
JW
Littlechild
J A
JA
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
D005656:Fungal Proteins; D005988:Glyceric Acids; D013431:Sulfates; C005156:3-phosphoglycerate; D010736:Phosphoglycerate Mutase