6ZN1

Trehalose transferase bound to alpha-D-glucopyranosyl-beta-galactopyranose from Thermoproteus uzoniensis

これはPDB形式変換不可エントリーです。

6ZN1 の概要

• エントリーDOI: 10.2210/pdb6zn1/pdb
• 分子名称: Trehalose phosphorylase/synthase, THIOCYANATE ION, DI(HYDROXYETHYL)ETHER, ... (6 entities in total)
• 機能のキーワード: trehalose transferase, retaining glycosyltransferase, glycosidic bond formation, transferase
• 由来する生物種: Thermoproteus uzoniensis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 46414.32

構造登録者

Bento, I.,Mestrom, L.,Marsden, S.R.,van der Eijk, H.,Laustsen, J.U.,Jeffries, C.M.,Svergun, D.I.,Hagedoorn, P.-H.,Hanefeld, U. (登録日: 2020-07-06, 公開日: 2021-01-20, 最終更新日: 2024-05-01)

主引用文献

Mestrom, L.,Marsden, S.R.,van der Eijk, H.,Laustsen, J.U.,Jeffries, C.M.,Svergun, D.I.,Hagedoorn, P.L.,Bento, I.,Hanefeld, U.
Anomeric Selectivity of Trehalose Transferase with Rare l-Sugars.
ACS Catal, 10:8835-8839, 2020

PubMed Abstract: Retaining LeLoir glycosyltransferases catalyze the formation of glycosidic bonds between nucleotide sugar donors and carbohydrate acceptors. The anomeric selectivity of trehalose transferase from was investigated for both d- and l-glycopyranose acceptors. The enzyme couples a wide range of carbohydrates, yielding trehalose analogues with conversion and enantioselectivity of >98%. The anomeric selectivity inverts from α,α-(1 → 1)-glycosidic bonds for d-glycopyranose acceptors to α,β-(1 → 1)-glycosidic bonds for l-glycopyranose acceptors, while ()-selectivity was retained for both types of sugar acceptors. Comparison of protein crystal structures of trehalose transferase in complex with α,α-trehalose and an unnatural α,β-trehalose analogue highlighted the mechanistic rationale for the observed inversion of anomeric selectivity.

PubMed: 32953231
DOI: 10.1021/acscatal.0c02117

実験手法

X-RAY DIFFRACTION (1.75 Å)