3ckv | pdb_00003ckv

Crystal Structure of a Mycobacterial Protein

spinqualitylabelsall models 3ckv, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ckv is a 1 chain structure with sequence from Mycobacterium paratuberculosis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, SO4, UDP Related: 3ckj, 3ckn, 3kco, 3kcq Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [GPGS_MYCPA] Involved in the biosynthesis of methylglucose lipopolysaccharides (MGLPs). Catalyzes the condensation of UDP-glucose and 3-phospho-glycerate (3-PGA) to yield glucosyl-3-phosphoglycerate (GPG). Although UDP-glucose is the natural donor sugar, GpgS can also use UDP-GalNAc, UDPGlcNAc, UDP-alpha-L-arabinose, UDP-Gal, UDP-Glc, UDP-alpha-Dglucuronic acid, and UDP-alpha-D-xylose as donor substrates. 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 Glycosyltransferases (GTs) are a large and ubiquitous family of enzymes that specifically transfer sugar moieties to a range of substrates. Mycobacterium tuberculosis contains a large number of GTs, many of which are implicated in cell wall synthesis, yet the majority of these GTs remain poorly characterized. Here, we report the high resolution crystal structures of an essential GT (MAP2569c) from Mycobacterium avium subsp. paratuberculosis (a close homologue of Rv1208 from M. tuberculosis) in its apo- and ligand-bound forms. The structure adopted the GT-A fold and possessed the characteristic DXD motif that coordinated an Mn(2+) ion. Atypical of most GTs characterized to date, MAP2569c exhibited specificity toward the donor substrate, UDP-glucose. The structure of this ligated complex revealed an induced fit binding mechanism and provided a basis for this unique specificity. Collectively, the structural features suggested that MAP2569c may adopt a "retaining" enzymatic mechanism, which has implications for the classification of other GTs in this large superfamily. Crystal structure of a UDP-glucose-specific glycosyltransferase from a Mycobacterium species.,Fulton Z, McAlister A, Wilce MC, Brammananth R, Zaker-Tabrizi L, Perugini MA, Bottomley SP, Coppel RL, Crellin PK, Rossjohn J, Beddoe T J Biol Chem. 2008 Oct 10;283(41):27881-90. Epub 2008 Jul 30. PMID:18667419 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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