8Z2Q

Crystal structure of trehalose synthase mutant N253Q from Deinococcus radiodurans

8Z2Q の概要

• エントリーDOI: 10.2210/pdb8z2q/pdb
• 分子名称: maltose alpha-D-glucosyltransferase, CALCIUM ION, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: trehalose, isomerase
• 由来する生物種: Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 521629.29

構造登録者

Ye, L.C.,Chen, S.C. (登録日: 2024-04-13, 公開日: 2025-01-01)

主引用文献

Ye, L.C.,Chow, S.Y.,Chang, S.C.,Kuo, C.H.,Wang, Y.L.,Wei, Y.J.,Lee, G.C.,Liaw, S.H.,Chen, W.M.,Chen, S.C.
Structural and Mutational Analyses of Trehalose Synthase from Deinococcus radiodurans Reveal the Interconversion of Maltose-Trehalose Mechanism.
J.Agric.Food Chem., 72:18649-18657, 2024

PubMed Abstract: Trehalose synthase (TreS) catalyzes the reversible interconversion of maltose to trehalose, playing a vital role in trehalose production. Understanding the catalytic mechanism of TreS is crucial for optimizing the enzyme activity and enhancing its suitability for industrial applications. Here, we report the crystal structures of both the wild type and the E324D mutant of trehalose synthase in complex with the trehalose analogue, validoxylamine A. By employing structure-guided mutagenesis, we identified N253, E320, and E324 as crucial residues within the +1 subsite for isomerase activity. Based on these complex structures, we propose the catalytic mechanism underlying the reversible interconversion of maltose to trehalose. These findings significantly advance our comprehension of the reaction mechanism of TreS.

PubMed: 39109746
DOI: 10.1021/acs.jafc.4c03661

実験手法

X-RAY DIFFRACTION (2.99 Å)