4RIE
Landomycin Glycosyltransferase LanGT2
4RIE の概要
| エントリーDOI | 10.2210/pdb4rie/pdb |
| 分子名称 | Glycosyl transferase homolog (2 entities in total) |
| 機能のキーワード | gt fold, glycosyltransferase, transferase |
| 由来する生物種 | Streptomyces cyanogenus |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 80812.21 |
| 構造登録者 | Tam, H.K.,Gerhardt, S.,Breit, B.,Bechthold, A.,Einsle, O. (登録日: 2014-10-06, 公開日: 2015-01-28, 最終更新日: 2023-09-20) |
| 主引用文献 | Tam, H.K.,Harle, J.,Gerhardt, S.,Rohr, J.,Wang, G.,Thorson, J.S.,Bigot, A.,Lutterbeck, M.,Seiche, W.,Breit, B.,Bechthold, A.,Einsle, O. Structural Characterization of O- and C-Glycosylating Variants of the Landomycin Glycosyltransferase LanGT2. Angew.Chem.Int.Ed.Engl., 54:2811-2815, 2015 Cited by PubMed Abstract: The structures of the O-glycosyltransferase LanGT2 and the engineered, C-C bond-forming variant LanGT2S8Ac show how the replacement of a single loop can change the functionality of the enzyme. Crystal structures of the enzymes in complex with a nonhydrolyzable nucleotide-sugar analogue revealed that there is a conformational transition to create the binding sites for the aglycon substrate. This induced-fit transition was explored by molecular docking experiments with various aglycon substrates. PubMed: 25581707DOI: 10.1002/anie.201409792 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.162 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






