期刊
STRUCTURE
卷 16, 期 6, 页码 965-975出版社
CELL PRESS
DOI: 10.1016/j.str.2008.03.010
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资金
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [U54GM074958, R01GM033225, R37GM033225, R01GM068692] Funding Source: NIH RePORTER
- NCRR NIH HHS [RR 005351] Funding Source: Medline
- NIGMS NIH HHS [U54 GM074958-030006, GM 068692, U54 GM 074958, GM 033225, R37 GM033225, R01 GM068692, R01 GM033225, R01 GM068692-04, R37 GM033225-24, U54 GM074958] Funding Source: Medline
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-GIcNAc, 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.
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