2jzc

NMR solution structure of ALG13: The sugar donor subunit of a yeast N-acetylglucosamine transferase. Northeast Structural Genomics Consortium target YG1

spinqualitylabelsall models 2jzc, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2jzc is a 1 chain structure with sequence from Atcc 18824. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: ALG13, YGL047W (ATCC 18824) Activity: N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase, with EC number 2.4.1.141 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN Function [ALG13_YEAST] Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. 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 solution structure of Alg13, the glycosyl donor-binding domain of an important bipartite glycosyltransferase in the yeast Saccharomyces cerevisiae, is presented. This glycosyltransferase is unusual in that it is active only in the presence of a binding partner, Alg14. Alg13 is found to adopt a unique topology among glycosyltransferases. Rather than the conventional Rossmann fold found in all GT-B enzymes, the N-terminal half of the protein is a Rossmann-like fold with a mixed parallel and antiparallel beta sheet. The Rossmann fold of the C-terminal half of Alg13 is conserved. However, although conventional GT-B enzymes usually possess three helices at the C terminus, only two helices are present in Alg13. Titration of Alg13 with both UDP-GlcNAc, the native glycosyl donor, and a paramagnetic mimic, UDP-TEMPO, shows that the interaction of Alg13 with the sugar donor is primarily through the residues in the C-terminal half of the protein. Solution structure of Alg13: the sugar donor subunit of a yeast N-acetylglucosamine transferase.,Wang X, Weldeghiorghis T, Zhang G, Imperiali B, Prestegard JH Structure. 2008 Jun;16(6):965-75. PMID:18547528 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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