View source for 6krl


==Crystal structure of GH30 xylanase B from Talaromyces cellulolyticus expressed by Pichia pastoris==
<StructureSection load='6krl' size='340' side='right'caption='[[6krl]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KRL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KRL 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]] 1.601&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=6krl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6krl OCA], [https://pdbe.org/6krl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6krl RCSB], [https://www.ebi.ac.uk/pdbsum/6krl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6krl ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Xylanase B, a member of subfamily 7 of the GH30 (glycoside hydrolase family 30) from Talaromyces cellulolyticus (TcXyn30B), is a bifunctional enzyme with glucuronoxylanase and xylobiohydrolase activities. In the present study, crystal structures of the native enzyme and the enzyme-product complex of TcXyn30B expressed in Pichia pastoris were determined at resolutions of 1.60 and 1.65 A, respectively. The enzyme complexed with 2(2) -(4-O-methyl-alpha-d-glucuronyl)-xylobiose (U(4m2) X) revealed that TcXyn30B strictly recognizes both the C-6 carboxyl group and the 4-O-methyl group of the 4-O-methyl-alpha-d-glucuronyl side chain by the conserved residues in GH30-7 endoxylanases. The crystal structure and site-directed mutagenesis indicated that Asn-93 on the beta2-alpha2-loop interacts with the non-reducing end of the xylose residue at subsite-2 and is likely to be involved in xylobiohydrolase activity. These findings provide structural insight into the mechanisms of substrate recognition of GH30-7 glucuronoxylanase and xylobiohydrolase.

Substrate recognition by a bifunctional GH30-7 xylanase B from Talaromyces cellulolyticus.,Nakamichi Y, Watanabe M, Matsushika A, Inoue H FEBS Open Bio. 2020 Jun;10(6):1180-1189. doi: 10.1002/2211-5463.12873. Epub 2020 , May 22. PMID:32359208<ref>PMID:32359208</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6krl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Inoue H]]
[[Category: Nakamichi Y]]
[[Category: Watanabe M]]