6krn
From Proteopedia
(Difference between revisions)
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==Crystal structure of GH30 xylanase B from Talaromyces cellulolyticus expressed by Pichia pastoris in complex with aldotriuronic acid== | ==Crystal structure of GH30 xylanase B from Talaromyces cellulolyticus expressed by Pichia pastoris in complex with aldotriuronic acid== | ||
| - | <StructureSection load='6krn' size='340' side='right'caption='[[6krn]]' scene=''> | + | <StructureSection load='6krn' size='340' side='right'caption='[[6krn]], [[Resolution|resolution]] 1.65Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KRN OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6krn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_uvarum Saccharomyces uvarum] and [https://en.wikipedia.org/wiki/Talaromyces_cellulolyticus_CF-2612 Talaromyces cellulolyticus CF-2612]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KRN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KRN FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.653Å</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=GCV:4-O-METHYL-ALPHA-D-GLUCURONIC+ACID'>GCV</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=XYP:BETA-D-XYLOPYRANOSE'>XYP</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=6krn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6krn OCA], [https://pdbe.org/6krn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6krn RCSB], [https://www.ebi.ac.uk/pdbsum/6krn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6krn ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A510NXC4_TALPI A0A510NXC4_TALPI] | ||
| + | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6krn" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomyces uvarum]] | ||
| + | [[Category: Talaromyces cellulolyticus CF-2612]] | ||
[[Category: Inoue H]] | [[Category: Inoue H]] | ||
[[Category: Nakamichi Y]] | [[Category: Nakamichi Y]] | ||
[[Category: Watanabe M]] | [[Category: Watanabe M]] | ||
Current revision
Crystal structure of GH30 xylanase B from Talaromyces cellulolyticus expressed by Pichia pastoris in complex with aldotriuronic acid
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