4cjb | pdb_00004cjb

orthorhombic crystal form of Bogt6a E192Q in complex with GalNAc

spinqualitylabelsall models 4cjb, resolution 2.78Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4cjb is a 4 chain structure with sequence from "bacteroides_fragilis_subsp._ovatus"_(eggerth_and_gagnon_1933)_holdeman_and_moore_1970 "bacteroides fragilis subsp. ovatus" (eggerth and gagnon 1933) holdeman and moore 1970. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: A2G Related: 4cj8, 4cjc Activity: Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase, with EC number 2.4.1.40 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Mammalian members of glycosyltransferase family 6 (GT6) of the CAZy database have a GT-A fold containing a conserved Asp-X-Asp (DXD) sequence that binds an essential metal cofactor. B. ovatus GT6a represents a GT6 clade found in more than 30 Gram-negative bacteria that is similar in sequence to the catalytic domains of mammalian GT6, but has an Asn95-Ala-Asn97 (NXN) sequence substituted for the DXD motif and metal-independent catalytic activity. Co-crystals of a low activity mutant of BoGT6a (Glu192Gln) with UDP-GalNAc contained protein complexes with intact UDP-GalNAc and two forms with hydrolysis products (UDP plus GalNAc) representing an initial closed complex and later open form primed for product release. Two cationic residues near the C-terminus of BoGT6a, Lys231 and Arg243, interact with the diphosphate moiety of UDP-GalNAc, but only Lys231 interacts with the UDP product and may function in leaving group stabilization. The amide group of Asn95, the first Asn of the NXN motif, interacts with the ribose moiety of the substrate. This metal-independent GT6 resembles its metal-dependent homologs in undergoing conformational changes on binding UDP-GalNAc that arise from structuring the C-terminus to cover this substrate. It appears that in the GT6 family the metal cofactor functions specifically in binding the UDP moiety in the donor substrate and transition state, actions that can be efficiently performed by components of the polypeptide chain. Structures of complexes of a metal-independent glycosyltransferase GT6 from Bacteroides ovatus with UDP-GalNAc and its hydrolysis products.,Pham TT, Stinson B, Thiyagarajan N, Lizotte-Waniewski M, Brew K, Acharya KR J Biol Chem. 2014 Jan 23. PMID:24459149 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glycosyltransferase

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