TY - JOUR
T1 - Solution Structure of Alg13
T2 - The Sugar Donor Subunit of a Yeast N-Acetylglucosamine Transferase
AU - Wang, Xu
AU - Weldeghiorghis, Thomas
AU - Zhang, Guofeng
AU - Imperiali, Barbara
AU - Prestegard, James H.
N1 - Funding Information:
This work is supported by the National Institutes of Health (grants GM033225 and RR005351 to J.H.P., grant GM068692 to B.I., and grant U54-GM074958 in support of the Northeast Structural Genomics Consortium) and by Fellowships from Alberta Heritage Foundation for Medical Research and Canadian Institutes for Health Research (support to X.W.). We also thank Fang Tian of University of Georgia for contributing the CCH-TOCSY pulse sequence and numerous insightful discussions, Jeffery Urbauer of University of Georgia for performing the sedimentation equilibrium experiment as well as assistance in analyzing the data, and Geert-Jan Boons and Andre Venot for the synthesis of UDP-TEMPO.
PY - 2008/6/11
Y1 - 2008/6/11
N2 - 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.
AB - 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.
KW - PROTEINS
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U2 - 10.1016/j.str.2008.03.010
DO - 10.1016/j.str.2008.03.010
M3 - Article
C2 - 18547528
AN - SCOPUS:44649191755
SN - 0969-2126
VL - 16
SP - 965
EP - 975
JO - Structure
JF - Structure
IS - 6
ER -