Solution structure of Alg13: the sugar donor subunit of a yeast N-acetylglucosamine transferase.
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.
Mesh Terms:
Amino Acid Sequence, Binding Sites, Cyclic N-Oxides, Ligands, Models, Molecular, Molecular Sequence Data, N-Acetylglucosaminyltransferases, Nuclear Magnetic Resonance, Biomolecular, Protein Structure, Secondary, Protein Subunits, Saccharomyces cerevisiae Proteins, Uridine Diphosphate, Uridine Diphosphate N-Acetylglucosamine
Amino Acid Sequence, Binding Sites, Cyclic N-Oxides, Ligands, Models, Molecular, Molecular Sequence Data, N-Acetylglucosaminyltransferases, Nuclear Magnetic Resonance, Biomolecular, Protein Structure, Secondary, Protein Subunits, Saccharomyces cerevisiae Proteins, Uridine Diphosphate, Uridine Diphosphate N-Acetylglucosamine
Structure
Date: Jun. 01, 2008
PubMed ID: 18547528
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