Structural highlights
Function
ALG13_YEAST Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Solution structure of Alg13: the sugar donor subunit of a yeast N-acetylglucosamine transferase.,Wang X, Weldeghiorghis T, Zhang G, Imperiali B, Prestegard JH Structure. 2008 Jun;16(6):965-75. PMID:18547528[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chantret I, Dancourt J, Barbat A, Moore SE. Two proteins homologous to the N- and C-terminal domains of the bacterial glycosyltransferase Murg are required for the second step of dolichyl-linked oligosaccharide synthesis in Saccharomyces cerevisiae. J Biol Chem. 2005 Mar 11;280(10):9236-42. Epub 2004 Dec 22. PMID:15615718 doi:http://dx.doi.org/M413941200
- ↑ Gao XD, Tachikawa H, Sato T, Jigami Y, Dean N. Alg14 recruits Alg13 to the cytoplasmic face of the endoplasmic reticulum to form a novel bipartite UDP-N-acetylglucosamine transferase required for the second step of N-linked glycosylation. J Biol Chem. 2005 Oct 28;280(43):36254-62. Epub 2005 Aug 12. PMID:16100110 doi:http://dx.doi.org/M507569200
- ↑ Wang X, Weldeghiorghis T, Zhang G, Imperiali B, Prestegard JH. Solution structure of Alg13: the sugar donor subunit of a yeast N-acetylglucosamine transferase. Structure. 2008 Jun;16(6):965-75. PMID:18547528 doi:10.1016/j.str.2008.03.010
