3H4I

Chimeric Glycosyltransferase for the generation of novel natural products

3H4I の概要

• エントリーDOI: 10.2210/pdb3h4i/pdb
• 関連するPDBエントリー: 3H4T
• 分子名称: Glycosyltransferase GtfA, Glycosyltransferase, URIDINE-5'-DIPHOSPHATE-2-DEOXY-2-FLUORO-ALPHA-D-GLUCOSE, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: glycosyltransferase, gtfa, chimeric protein, vancomycin, teicoplanin, antibiotic, transferase
• 由来する生物種: Amycolatopsis orientalis; 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 42868.00

構造登録者

Dias, M.V.B.,Truman, A.W.,Wu, S.,Blundell, T.L.,Huang, F.,Spencer, J.B. (登録日: 2009-04-20, 公開日: 2009-07-28, 最終更新日: 2023-11-01)

主引用文献

Truman, A.W.,Dias, M.V.B.,Wu, S.,Blundell, T.L.,Huang, F.,Spencer, J.B.
Chimeric glycosyltransferases for the generation of hybrid glycopeptides
Chem.Biol., 16:676-685, 2009

PubMed Abstract: Glycodiversification, an invaluable tool for generating biochemical diversity, can be catalyzed by glycosyltransferases, which attach activated sugar "donors" onto "acceptor" molecules. However, many glycosyltransferases can tolerate only minor modifications to their native substrates, thus making them unsuitable tools for current glycodiversification strategies. Here we report the production of functional chimeric glycosyltransferases by mixing and matching the N- and C-terminal domains of glycopeptide glycosyltransferases. Using this method we have generated hybrid glycopeptides and have demonstrated that domain swapping can result in a predictable switch of substrate specificity, illustrating that N- and C-terminal domains predominantly dictate acceptor and donor specificity, respectively. The determination of the structure of a chimera in complex with a sugar donor analog shows that almost all sugar-glycosyltransferase binding interactions occur in the C-terminal domain.

PubMed: 19549605
DOI: 10.1016/j.chembiol.2009.04.013

実験手法

X-RAY DIFFRACTION (1.3 Å)