8Z2T
Crystal structure of trehalose synthase from Deinococcus radiodurans complexed with validoxylamine A (VAA)
Summary for 8Z2T
| Entry DOI | 10.2210/pdb8z2t/pdb |
| Descriptor | maltose alpha-D-glucosyltransferase, CALCIUM ION, MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | trehalose, isomerase |
| Biological source | Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539 |
| Total number of polymer chains | 4 |
| Total formula weight | 261550.31 |
| Authors | |
| 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 Cited by 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: 39109746DOI: 10.1021/acs.jafc.4c03661 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.83 Å) |
Structure validation
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