5x7u
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Trehalose synthase from Thermobaculum terrenum== | |
| + | <StructureSection load='5x7u' size='340' side='right' caption='[[5x7u]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5x7u]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X7U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5X7U FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5x7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x7u OCA], [http://pdbe.org/5x7u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x7u RCSB], [http://www.ebi.ac.uk/pdbsum/5x7u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x7u ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Trehalose has important applications in the food industry and pharmaceutical manufacturing. The thermostable enzyme trehalose synthase from Thermobaculum terrenum (TtTS) catalyzes the reversible interconversion of maltose and trehalose. Here, we investigated the structural characteristics of TtTS in complex with the inhibitor TriS. TtTS exhibits the typical three domain glycoside hydrolase family 13 structure. The catalytic cleft consists of Asp202-Glu244-Asp310 and various conserved substrate-binding residues. However, among trehalose synthases, TtTS demonstrates obvious thermal stability. TtTS has more polar (charged) amino acids distributed on its protein structure surface and more aromatic amino acids buried within than other mesophilic trehalose synthases. Furthermore, TtTS structural analysis revealed four potential metal ion-binding sites rather than the two in a homologous structure. These factors may render TtTS relatively more thermostable among mesophilic trehalose synthases. The detailed thermophilic enzyme structure provided herein may provide guidance for further protein engineering in the design of stabilized enzymes. | ||
| - | + | Structural Characteristics and Function of a New Kind of Thermostable Trehalose Synthase from Thermobaculum terrenum.,Wang J, Ren X, Wang R, Su J, Wang F J Agric Food Chem. 2017 Sep 6;65(35):7726-7735. doi: 10.1021/acs.jafc.7b02732., Epub 2017 Aug 23. PMID:28809106<ref>PMID:28809106</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5x7u" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Su, J]] | ||
| + | [[Category: Wang, F]] | ||
| + | [[Category: Complex]] | ||
| + | [[Category: Gh13 family]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Trehalose synathase]] | ||
Revision as of 06:27, 28 February 2018
Trehalose synthase from Thermobaculum terrenum
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Categories: Su, J | Wang, F | Complex | Gh13 family | Hydrolase | Trehalose synathase
