2JZC
NMR solution structure of ALG13: The sugar donor subunit of a yeast N-acetylglucosamine transferase. Northeast Structural Genomics Consortium target YG1
Summary for 2JZC
| Entry DOI | 10.2210/pdb2jzc/pdb |
| NMR Information | BMRB: 15617 |
| Descriptor | UDP-N-acetylglucosamine transferase subunit ALG13 (1 entity in total) |
| Functional Keywords | rossmann-like fold, endoplasmic reticulum, glycosyltransferase, transferase, structural genomics, psi-2, protein structure initiative, northeast structural genomics consortium, nesg |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 25097.67 |
| Authors | Wang, X.,Weldeghorghis, T.,Zhang, G.,Imepriali, B.,Montelione, G.T.,Prestegard, J.H.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2008-01-04, release date: 2008-02-19, Last modification date: 2024-05-08) |
| Primary citation | Wang, X.,Weldeghiorghis, T.,Zhang, G.,Imperiali, B.,Prestegard, J.H. Solution structure of Alg13: the sugar donor subunit of a yeast N-acetylglucosamine transferase. Structure, 16:965-975, 2008 Cited by PubMed Abstract: 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. PubMed: 18547528DOI: 10.1016/j.str.2008.03.010 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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