1o99
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CRYSTAL STRUCTURE OF THE S62A MUTANT OF PHOSPHOGLYCERATE MUTASE FROM BACILLUS STEAROTHERMOPHILUS COMPLEXED WITH 2-PHOSPHOGLYCERATE
OverviewOverview
Phosphoglycerate mutases catalyze the isomerization of 2 and, 3-phosphoglycerates, and are essential for glucose metabolism in most, organisms. Here, we further characterize the, 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (iPGM) from, Bacillus stearothermophilus by determination of a high-resolution (1.4A), crystal structure of the wild-type enzyme and the crystal structure of its, S62A mutant. The mutant structure surprisingly showed the replacement of, one of the two catalytically essential manganese ions with a water, molecule, offering an additional possible explanation for its lack of, catalytic activity. Crystal structures invariably show substrate, phosphoglycerate to be entirely buried in a deep cleft between the two, iPGM domains. Flexibility analyses were ... [(full description)]
About this StructureAbout this Structure
1O99 is a [Single protein] structure of sequence from [Geobacillus stearothermophilus] with MN, SO4 and 2PG as [ligands]. Active as [Phosphoglycerate mutase], with EC number [5.4.2.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Insights into the catalytic mechanism of cofactor-independent phosphoglycerate mutase from X-ray crystallography, simulated dynamics and molecular modeling., Rigden DJ, Lamani E, Mello LV, Littlejohn JE, Jedrzejas MJ, J Mol Biol. 2003 May 9;328(4):909-20. PMID:12729763
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