|Structure (2008) 16:965-75|
|Northeast Structural Genomics Consortium|
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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.
|chemistry analogs & derivatives |
|Models, Molecular Uridine Diphosphate N-Acetylglucosamine Saccharomyces cerevisiae Proteins Molecular Sequence Data Ligands Protein Subunits Binding Sites Protein Structure, Secondary Amino Acid Sequence Cyclic N-Oxides Nuclear Magnetic Resonance, Biomolecular N-Acetylglucosaminyltransferases Uridine Diphosphate |
|18 (Last update: 04/21/2018 3:14:05pm)|