5jud | pdb_00005jud

Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with uridine-diphosphate (UDP) - GpgS*UDP

spinqualitylabelsall models 5jud, resolution 2.59Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5jud is a 1 chain structure with sequence from Mycobacterium tuberculosis variant bovis AF2122/97. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.59Å Ligands: UDP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GPGS_MYCBO 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). It can use UDP-glucose, ADP-glucose and GDP-glucose as donor substrates with decreasing affinity, and 3-PGA as an acceptor. D-glycerate could only be the acceptor with ADP-glucose and at a very low rate. Publication Abstract from PubMed Glycosyltransferases (GTs) play a central role in nature. They catalyze the transfer of a sugar moiety to a broad range of acceptor substrates. GTs are highly selective enzymes, allowing the recognition of subtle structural differences in the sequences and stereochemistry of their sugar and acceptor substrates. We report here a series of structural snapshots of the reaction center of the retaining glucosyl-3-phosphoglycerate synthase (GpgS). During this sequence of events, we visualize how the enzyme guides the substrates into the reaction center where the glycosyl transfer reaction takes place, and unveil the mechanism of product release, involving multiple conformational changes not only in the substrates/products but also in the enzyme. The structural data are further complemented by metadynamics free-energy calculations, revealing how the equilibrium of loop conformations is modulated along these itineraries. The information reported here represent an important contribution for the understanding of GT enzymes at the molecular level. Structural Snapshots and Loop Dynamics along the Catalytic Cycle of Glycosyltransferase GpgS.,Albesa-Jove D, Romero-Garcia J, Sancho-Vaello E, Contreras FX, Rodrigo-Unzueta A, Comino N, Carreras-Gonzalez A, Arrasate P, Urresti S, Biarnes X, Planas A, Guerin ME Structure. 2017 Jul 5;25(7):1034-1044.e3. doi: 10.1016/j.str.2017.05.009. Epub, 2017 Jun 15. PMID:28625787 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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