Acta Crystallographica Section D Biological Crystallography · 1999 · 21 citations · 12 references
Life SciencesBiochemistryMolecular BiologyEnzymologyStructural BiochemistryStructural BiologyEnzyme Active SitesEnzyme BiophysicsEnzyme FunctionEnzyme StructureEnzyme-substrate RecognitionStructural EnzymologyGlycolipid BiosynthesisPhosphoglycerate KinaseSugar-phosphate Backbone
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.
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T. Alwyn Jones, Jin-yu Zou, Sandra W. Cowan et al. · Acta Crystallographica Section A Foundations of Crystallography · 1991 · 12.7K citations