8z2r: Difference between revisions
New page: '''Unreleased structure''' The entry 8z2r is ON HOLD until Paper Publication Authors: Ye, L.C., Chen, S.C. Description: Crystal structure of trehalose synthase mutant N253T from Deinoc... |
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==Crystal structure of trehalose synthase mutant N253T from Deinococcus radiodurans== | |||
<StructureSection load='8z2r' size='340' side='right'caption='[[8z2r]], [[Resolution|resolution]] 2.53Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8z2r]] 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=8Z2R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8Z2R 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]] 2.53Å</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=8z2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8z2r OCA], [https://pdbe.org/8z2r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8z2r RCSB], [https://www.ebi.ac.uk/pdbsum/8z2r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8z2r 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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Chen | <div class="pdbe-citations 8z2r" style="background-color:#fffaf0;"></div> | ||
[[Category: Ye | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Deinococcus radiodurans R1]] | |||
[[Category: Large Structures]] | |||
[[Category: Chen SC]] | |||
[[Category: Ye LC]] | |||
Latest revision as of 17:00, 1 January 2025
Crystal structure of trehalose synthase mutant N253T from Deinococcus radioduransCrystal structure of trehalose synthase mutant N253T from Deinococcus radiodurans
Structural highlights
FunctionPublication Abstract from PubMedTrehalose 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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