NMR solution structure of ALG13: The sugar donor subunit of a yeast N-acetylglucosamine transferase. Northeast Structural Genomics Consortium target YG1
2jzc is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑Wang X, Weldeghiorghis T, Zhang G, Imperiali B, Prestegard JH. Solution structure of Alg13: the sugar donor subunit of a yeast N-acetylglucosamine transferase. Structure. 2008 Jun;16(6):965-75. PMID:18547528 doi:10.1016/j.str.2008.03.010
