Solution Structure of Alg13: The Sugar Donor Subunit of a Yeast N-Acetylglucosamine Transferase

Xu Wang, Thomas Weldeghiorghis, Guofeng Zhang, Barbara Imperiali, James H. Prestegard

Research output: Contribution to journalArticlepeer-review

27 Scopus citations


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 β 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.

Original languageEnglish (US)
Pages (from-to)965-975
Number of pages11
Issue number6
StatePublished - Jun 11 2008
Externally publishedYes



ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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