4y9x

Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with Mn2+, uridine-diphosphate-glucose (UDP-Glc) and phosphoglyceric acid (PGA) - GpgS Mn2+ UDP-Glc PGA-3

spinqualitylabelsall models 4y9x, resolution 2.64Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4y9x is a 1 chain structure with sequence from Mycobacterium tuberculosis H37Rv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.637Å Ligands: 3PG, CL, EDO, MN, UPG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GPGS_MYCTU Involved in the biosynthesis of methylglucose lipopolysaccharides (MGLPs). Catalyzes the condensation of NDP-glucose and 3-phospho-glycerate (3-PGA) to yield glucosyl-3-phosphoglycerate (GPG). Publication Abstract from PubMed Glycosyltransferases (GTs) comprise a prominent family of enzymes that play critical roles in a variety of cellular processes, including cell signaling, cell development, and host-pathogen interactions. Glycosyl transfer can proceed with either inversion or retention of the anomeric configuration with respect to the reaction substrates and products. The elucidation of the catalytic mechanism of retaining GTs remains a major challenge. A native ternary complex of a GT in a productive mode for catalysis is reported, that of the retaining glucosyl-3-phosphoglycerate synthase GpgS from M. tuberculosis in the presence of the sugar donor UDP-Glc, the acceptor substrate phosphoglycerate, and the divalent cation cofactor. Through a combination of structural, chemical, enzymatic, molecular dynamics, and quantum-mechanics/molecular-mechanics (QM/MM) calculations, the catalytic mechanism was unraveled, thereby providing a strong experimental support for a front-side substrate-assisted SN i-type reaction. A Native Ternary Complex Trapped in a Crystal Reveals the Catalytic Mechanism of a Retaining Glycosyltransferase.,Albesa-Jove D, Mendoza F, Rodrigo-Unzueta A, Gomollon-Bel F, Cifuente JO, Urresti S, Comino N, Gomez H, Romero-Garcia J, Lluch JM, Sancho-Vaello E, Biarnes X, Planas A, Merino P, Masgrau L, Guerin ME Angew Chem Int Ed Engl. 2015 Jul 1. doi: 10.1002/anie.201504617. PMID:26136334 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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