View source for 5xgz


==Metagenomic glucose-tolerant glycosidase==
<StructureSection load='5xgz' size='340' side='right'caption='[[5xgz]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5xgz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Uncultured_microorganism Uncultured microorganism]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XGZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XGZ 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]] 1.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5xgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xgz OCA], [https://pdbe.org/5xgz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xgz RCSB], [https://www.ebi.ac.uk/pdbsum/5xgz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xgz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1E1FFN6_9ZZZZ A0A1E1FFN6_9ZZZZ] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
MeBglD2, a metagenomic beta-glycosidase, is stimulated by various saccharides, including D-glucose, D-xylose, and maltose, and it promotes the enzymatic saccharification of plant biomass. To improve the thermostability of MeBglD2, its X-ray crystal structure was analyzed, and the amino acid residues responsible for its thermostability were identified using the structural information. Mutations in His8, Asn59, and Gly295 improved the thermostability of MeBglD2, and the combination of these mutations resulted in the highest thermostability. Compared with wild-type MeBglD2, thermostable MeBglD2 mutants promoted plant biomass saccharification using Trichoderma reesei cellulase. In addition to thermostability, the thermostable mutants exhibited higher tolerance to ethanol, dimethyl sulfoxide, and copper ions, indicating that the MeBglD2 mutants generated in this study were improved in their tolerance to not only high temperature but also to organic solvents and metal ions.

Improved thermostability of a metagenomic glucose-tolerant beta-glycosidase based on its X-ray crystal structure.,Matsuzawa T, Watanabe M, Yaoi K Appl Microbiol Biotechnol. 2017 Dec;101(23-24):8353-8363. doi:, 10.1007/s00253-017-8525-9. Epub 2017 Oct 23. PMID:29063172<ref>PMID:29063172</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5xgz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Uncultured microorganism]]
[[Category: Matsuzawa T]]
[[Category: Watanabe M]]
[[Category: Yaoi K]]