2JZC

NMR solution structure of ALG13: The sugar donor subunit of a yeast N-acetylglucosamine transferase. Northeast Structural Genomics Consortium target YG1

2JZC の概要

• エントリーDOI: 10.2210/pdb2jzc/pdb
• NMR情報: BMRB: 15617
• 分子名称: UDP-N-acetylglucosamine transferase subunit ALG13 (1 entity in total)
• 機能のキーワード: rossmann-like fold, endoplasmic reticulum, glycosyltransferase, transferase, structural genomics, psi-2, protein structure initiative, northeast structural genomics consortium, nesg
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25097.67

構造登録者

Wang, X.,Weldeghorghis, T.,Zhang, G.,Imepriali, B.,Montelione, G.T.,Prestegard, J.H.,Northeast Structural Genomics Consortium (NESG) (登録日: 2008-01-04, 公開日: 2008-02-19, 最終更新日: 2024-05-08)

主引用文献

Wang, X.,Weldeghiorghis, T.,Zhang, G.,Imperiali, B.,Prestegard, J.H.
Solution structure of Alg13: the sugar donor subunit of a yeast N-acetylglucosamine transferase.
Structure, 16:965-975, 2008

PubMed Abstract: 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.

PubMed: 18547528
DOI: 10.1016/j.str.2008.03.010

実験手法

SOLUTION NMR