6m5z
From Proteopedia
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==Catalytic domain of GH30 xylanase C from Talaromyces cellulolyticus== | ==Catalytic domain of GH30 xylanase C from Talaromyces cellulolyticus== | ||
| - | <StructureSection load='6m5z' size='340' side='right'caption='[[6m5z]]' scene=''> | + | <StructureSection load='6m5z' size='340' side='right'caption='[[6m5z]], [[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=6M5Z OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6m5z]] is a 2 chain structure with sequence from [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=6M5Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6M5Z 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]] 1.65Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</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=6m5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m5z OCA], [https://pdbe.org/6m5z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6m5z RCSB], [https://www.ebi.ac.uk/pdbsum/6m5z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6m5z ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A6N4SL16_TALPI A0A6N4SL16_TALPI] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | GH30-7 endoxylanase C from the cellulolytic fungus Talaromyces cellulolyticus (TcXyn30C) belongs to glycoside hydrolase family 30 subfamily 7, and specifically releases 2(2)-(4-O-methyl-alpha-D-glucuronosyl)-xylobiose from glucuronoxylan, as well as various arabino-xylooligosaccharides from arabinoxylan. TcXyn30C has a modular structure consisting of a catalytic domain and a C-terminal cellulose-binding module 1 (CBM1). In this study, the crystal structure of a TcXyn30C mutant which lacks the CBM1 domain was determined at 1.65 A resolution. The structure of the active site of TcXyn30C was compared with that of the bifunctional GH30-7 xylanase B from T. cellulolyticus (TcXyn30B), which exhibits glucuronoxylanase and xylobiohydrolase activities. The results revealed that TcXyn30C has a conserved structural feature for recognizing the 4-O-methyl-alpha-D-glucuronic acid (MeGlcA) substituent in subsite -2b. Additionally, the results demonstrated that Phe47 contributes significantly to catalysis by TcXyn30C. Phe47 is located in subsite -2b and also near the C-3 hydroxyl group of a xylose residue in subsite -2a. Substitution of Phe47 with an arginine residue caused a remarkable decrease in the catalytic efficiency towards arabinoxylan, suggesting the importance of Phe47 in arabinoxylan hydrolysis. These findings indicate that subsite -2b of TcXyn30C has unique structural features that interact with arabinofuranose and MeGlcA substituents. | ||
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| + | Crystal structure of GH30-7 endoxylanase C from the filamentous fungus Talaromyces cellulolyticus.,Nakamichi Y, Fujii T, Watanabe M, Matsushika A, Inoue H Acta Crystallogr F Struct Biol Commun. 2020 Aug 1;76(Pt 8):341-349. doi:, 10.1107/S2053230X20009024. Epub 2020 Jul 28. PMID:32744245<ref>PMID:32744245</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6m5z" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Talaromyces cellulolyticus CF-2612]] | ||
[[Category: Inoue H]] | [[Category: Inoue H]] | ||
[[Category: Nakamichi Y]] | [[Category: Nakamichi Y]] | ||
[[Category: Watanabe M]] | [[Category: Watanabe M]] | ||
Revision as of 15:18, 29 November 2023
Catalytic domain of GH30 xylanase C from Talaromyces cellulolyticus
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