8Z2R

Crystal structure of trehalose synthase mutant N253T from Deinococcus radiodurans

Summary for 8Z2R

• Entry DOI: 10.2210/pdb8z2r/pdb
• Descriptor: maltose alpha-D-glucosyltransferase, CALCIUM ION, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: trehalose, isomerase
• Biological source: Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)
• Total number of polymer chains: 8
• Total formula weight: 521290.96

Authors

Ye, L.C.,Chen, S.C. (deposition date: 2024-04-13, release date: 2025-01-01)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.53 Å)