5x7u

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:17, 27 March 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='5x7u' size='340' side='right'caption='[[5x7u]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='5x7u' size='340' side='right'caption='[[5x7u]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== 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://proteopedia.org/fgij/fg.htm?mol=5X7U FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5x7u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermobaculum_terrenum_ATCC_BAA-798 Thermobaculum terrenum ATCC BAA-798]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5X7U FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.501&#8491;</td></tr>
-
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=5x7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x7u OCA], [https://pdbe.org/5x7u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5x7u RCSB], [https://www.ebi.ac.uk/pdbsum/5x7u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5x7u ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/D1CE96_THET1 D1CE96_THET1]
-
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 5x7u" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Su, J]]
+
[[Category: Thermobaculum terrenum ATCC BAA-798]]
-
[[Category: Wang, F]]
+
[[Category: Su J]]
-
[[Category: Complex]]
+
[[Category: Wang F]]
-
[[Category: Gh13 family]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: Trehalose synathase]]
+

Current revision

Trehalose synthase from Thermobaculum terrenum

PDB ID 5x7u

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5x7u"
Personal tools