1eqj

CRYSTAL STRUCTURE OF PHOSPHOGLYCERATE MUTASE FROM BACILLUS STEAROTHERMOPHILUS COMPLEXED WITH 2-PHOSPHOGLYCERATE

spinqualitylabelsall models 1eqj, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1eqj is a 1 chain structure. The February 2004 RCSB PDB Molecule of the Month feature on The Glycolytic Enzymes by David S. Goodsell is 10.2210/rcsb_pdb/mom_2004_2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 2PG, MN Related: 1ejj Activity: Phosphoglycerate mutase, with EC number 5.4.2.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [GPMI_GEOSE] Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.[HAMAP-Rule:MF_01038] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The structure of the complex between the 2, 3-diphosphoglycerate-independent phosphoglycerate mutase (iPGM) from Bacillus stearothermophilus and its 3-phosphoglycerate substrate has recently been solved, and analysis of this structure allowed formulation of a mechanism for iPGM catalysis. In order to obtain further evidence for this mechanism, we have solved the structure of this iPGM complexed with 2-phosphoglycerate and two Mn(2+) ions at 1. 7-A resolution. The structure consists of two different domains connected by two loops and interacting through a network of hydrogen bonds. This structure is consistent with the proposed mechanism for iPGM catalysis, with the two main steps in catalysis being a phosphatase reaction removing the phosphate from 2- or 3-phosphoglycerate, generating an enzyme-bound phosphoserine intermediate, followed by a phosphotransferase reaction as the phosphate is transferred from the enzyme back to the glycerate moiety. The structure also allowed the assignment of the function of the two domains of the enzyme, one of which participates in the phosphatase reaction and formation of the phosphoserine enzyme intermediate, with the other involved in the phosphotransferase reaction regenerating phosphoglycerate. Significant structural similarity has also been found between the active site of the iPGM domain catalyzing the phosphatase reaction and Escherichia coli alkaline phosphatase. Mechanism of catalysis of the cofactor-independent phosphoglycerate mutase from Bacillus stearothermophilus. Crystal structure of the complex with 2-phosphoglycerate.,Jedrzejas MJ, Chander M, Setlow P, Krishnasamy G J Biol Chem. 2000 Jul 28;275(30):23146-53. PMID:10764795 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phosphoglycerate Mutase

Proteopedia Page Contributors and Editors (what is this?)

OCA