View source for 5zqj


==Crystal structure of beta-xylosidase from Bacillus pumilus==
<StructureSection load='5zqj' size='340' side='right'caption='[[5zqj]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5zqj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_pumilus Bacillus pumilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZQJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZQJ 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]] 1.73&#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></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=5zqj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zqj OCA], [https://pdbe.org/5zqj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zqj RCSB], [https://www.ebi.ac.uk/pdbsum/5zqj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zqj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/XYNB_BACPU XYNB_BACPU] Beta-xylosidase is an intracellular xylan-degrading enzyme.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Xylobiose consists of two molecules of xylose and has been highly recognized as a food supplement because it possesses high prebiotic functions. beta-xylosidase exhibits enzymatic activity to hydrolyze xylobiose, and the enzyme can also catalyze the reverse reaction in the presence of high concentrations of xylose. Previously, beta-xylosidase from Bacillus pumilus IPO (BpXynB), belonging to GH family 43, was employed to produce xylobiose from xylose. To improve the enzymatic efficiency, this study determined the high-resolution structure of BpXynB in a complex with xylobiose and engineered BpXynB based on the structures. The structure of BpXynB deciphered the residues involved in the recognition of the xylobiose. A site-directed mutation at the residue for xylobiose recognition increased the yield of xylobiose by 20% compared to a similar activity of the wild type enzyme. The complex structure of the mutant enzyme and xylobiose provided the structural basis for a higher yield of the engineered protein. This engineered enzyme would enable a higher economic production of xylobiose, and a similar engineering strategy could be applied within the same family of enzymes.

Structure-based protein engineering of bacterial beta-xylosidase to increase the production yield of xylobiose from xylose.,Hong S, Kyung M, Jo I, Kim YR, Ha NC Biochem Biophys Res Commun. 2018 Jun 27;501(3):703-710. doi:, 10.1016/j.bbrc.2018.05.051. PMID:29752942<ref>PMID:29752942</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5zqj" style="background-color:#fffaf0;"></div>

==See Also==
*[[Xylosidase 3D structures|Xylosidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus pumilus]]
[[Category: Large Structures]]
[[Category: Ha NC]]
[[Category: Hong S]]
[[Category: Jo I]]