title: An ensemble of structures of Burkholderia pseudomallei 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase.
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.
authors: Seattle Structural Genomics Center for Infectious Disease (http://www.ssgcid.org), USA. ddavies@embios.com
authors: Douglas R
authors: DR
authors: Davies
authors: Bart L
authors: BL
authors: Staker
authors: Jan A
authors: JA
authors: Abendroth
authors: Thomas E
authors: TE
authors: Edwards
authors: Robert
authors: R
authors: Hartley
authors: Jess
authors: J
authors: Leonard
authors: Hidong
authors: H
authors: Kim
authors: Amanda L
authors: AL
authors: Rychel
authors: Stephen N
authors: SN
authors: Hewitt
authors: Peter J
authors: PJ
authors: Myler
authors: Lance J
authors: LJ
authors: Stewart
mesh_terms: D016957:Burkholderia pseudomallei / Q000201:enzymology*; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D010736:Phosphoglycerate Mutase / Q000737:chemistry* / Q000378:metabolism; D017434:Protein Structure, Tertiary; D013379:Substrate Specificity
chemical_list: D010736:Phosphoglycerate Mutase