PMID:21904048

Citation	Davies, DR, Staker, BL, Abendroth, JA, Edwards, TE, Hartley, R, Leonard, J, Kim, H, Rychel, AL, Hewitt, SN, Myler, PJ and Stewart, LJ (2011) An ensemble of structures of Burkholderia pseudomallei 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67:1044-50
Abstract	Burkholderia pseudomallei is a soil-dwelling bacterium endemic to Southeast Asia and Northern Australia. Burkholderia is responsible for melioidosis, a serious infection of the skin. The enzyme 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (PGAM) catalyzes the interconversion of 3-phosphoglycerate and 2-phosphoglycerate, a key step in the glycolytic pathway. As such it is an extensively studied enzyme and X-ray crystal structures of PGAM enzymes from multiple species have been elucidated. Vanadate is a phosphate mimic that is a powerful tool for studying enzymatic mechanisms in phosphoryl-transfer enzymes such as phosphoglycerate mutase. However, to date no X-ray crystal structures of phosphoglycerate mutase have been solved with vanadate acting as a substrate mimic. Here, two vanadate complexes together with an ensemble of substrate and fragment-bound structures that provide a comprehensive picture of the function of the Burkholderia enzyme are reported.
Links	PubMed PMC3169400 Online version:10.1107/S1744309111030405
Keywords	Burkholderia pseudomallei/enzymology; Crystallography, X-Ray; Models, Molecular; Phosphoglycerate Mutase/chemistry; Phosphoglycerate Mutase/metabolism; Protein Structure, Tertiary; Substrate Specificity
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