3LNT

Crystal structure of phosphoglyceromutase from Burkholderia Pseudomallei 1710B with bound malonic acid

Summary for 3LNT

• Entry DOI: 10.2210/pdb3lnt/pdb
• Related: 3EZN 3FDZ 3GP3 3GP5 3GW8
• Descriptor: 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase, SODIUM ION, MALONATE ION, ... (5 entities in total)
• Functional Keywords: mutase, phosphoglycerylmutase, seattle structural genomics center for infectious disease, ssgcid, glycolysis, isomerase
• Biological source: Burkholderia pseudomallei
• Total number of polymer chains: 2
• Total formula weight: 56442.81

Authors

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2010-02-03, release date: 2010-02-09, Last modification date: 2024-02-21)

Primary citation

Davies, D.R.,Staker, B.L.,Abendroth, J.A.,Edwards, T.E.,Hartley, R.,Leonard, J.,Kim, H.,Rychel, A.L.,Hewitt, S.N.,Myler, P.J.,Stewart, L.J.
An ensemble of structures of Burkholderia pseudomallei 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase.
Acta Crystallogr.,Sect.F, 67:1044-1050, 2011

PubMed 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.

PubMed: 21904048
DOI: 10.1107/S1744309111030405

Experimental method

X-RAY DIFFRACTION (2.1 Å)