Sulphate ions observed in the 2.12 Å structure of a new crystal form of S. cerevisiae phosphoglycerate mutase provide insights into understanding the catalytic mechanism

Journal of Molecular Biology

Volumn 286, Issue 5, 1999, Pages 1507-1517

  Rigden, Daniel J ^a,b   Walter, Rebecca A ^b   Phillips, Simon E V ^a   Fothergill Gilmore, Linda A ^a  

^a UNIVERSITY OF LEEDS   (United Kingdom)

^b UNIVERSITY OF EDINBURGH   (United Kingdom)

Author keywords

Active site sulphate ions; Crystal structure; Enzyme phosphorylation; Ligand binding; Phosphoglycerate mutase

Indexed keywords

ION; PHOSPHOGLYCERATE MUTASE; SULFATE;

ARTICLE; CRYSTAL STRUCTURE; ENZYME PHOSPHORYLATION; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; SACCHAROMYCES CEREVISIAE;

EID: 0033548451     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2566     Document Type: Article

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