8z2q: Difference between revisions

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-'''Unreleased structure'''
-The entry 8z2q is ON HOLD  until Paper Publication
+==Crystal structure of trehalose synthase mutant N253Q from Deinococcus radiodurans==
+<StructureSection load='8z2q' size='340' side='right'caption='[[8z2q]], [[Resolution|resolution]] 2.99&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8z2q]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans_R1 Deinococcus radiodurans R1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8Z2Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8Z2Q FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.99&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8z2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8z2q OCA], [https://pdbe.org/8z2q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8z2q RCSB], [https://www.ebi.ac.uk/pdbsum/8z2q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8z2q ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/I3NX86_DEIRA I3NX86_DEIRA]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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 Deinococcus radiodurans 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.
-Authors: Ye, L.C., Chen, S.C.
+Structural and Mutational Analyses of Trehalose Synthase from Deinococcus radiodurans Reveal the Interconversion of Maltose-Trehalose Mechanism.,Ye LC, Chow SY, Chang SC, Kuo CH, Wang YL, Wei YJ, Lee GC, Liaw SH, Chen WM, Chen SC J Agric Food Chem. 2024 Aug 21;72(33):18649-18657. doi: 10.1021/acs.jafc.4c03661. , Epub 2024 Aug 7. PMID:39109746<ref>PMID:39109746</ref>
-Description: Crystal structure of trehalose synthase mutant N253Q from Deinococcus radiodurans
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Chen, S.C]]
+<div class="pdbe-citations 8z2q" style="background-color:#fffaf0;"></div>
-[[Category: Ye, L.C]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Deinococcus radiodurans R1]]
+[[Category: Large Structures]]
+[[Category: Chen SC]]
+[[Category: Ye LC]]