7zsz

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<StructureSection load='7zsz' size='340' side='right'caption='[[7zsz]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='7zsz' size='340' side='right'caption='[[7zsz]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7zsz]] is a 2 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=7ayl 7ayl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZSZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZSZ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7zsz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Uncultured_bacterium_#0087-1D13 Uncultured bacterium #0087-1D13]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=7ayl 7ayl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZSZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZSZ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] </span></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=7zsz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zsz OCA], [https://pdbe.org/7zsz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zsz RCSB], [https://www.ebi.ac.uk/pdbsum/7zsz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zsz ProSAT]</span></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=7zsz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zsz OCA], [https://pdbe.org/7zsz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zsz RCSB], [https://www.ebi.ac.uk/pdbsum/7zsz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zsz ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[[https://www.uniprot.org/uniprot/A0A140HJ20_9BACT A0A140HJ20_9BACT]]
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The depletion of fossil fuels, associated pollution, and resulting health hazards are of concern worldwide. Woody biomass constitutes an alternative source of cleaner and renewable energy. The efficient use of woody biomass depends on xylan depolymerisation as the endo-beta-1,4-xylopyranosyl homopolymer is the main component of hemicellulose, the second most abundant component of wood. Xylan depolymerisation is achieved by hemicellulolytic xylanases of glycoside hydrolase (GH) families 5, 8, 10, 11, 30 and 43 of the CAZY database. We analysed a multidomain xylanase (Xyl) from the hindgut metagenome of the snouted harvester termite Trinervitermes trinervoides that releases xylobiose and xylotriose from beech and birch xylan and wheat arabinoxylan. The four domains of Xyl include an N-terminal GH11 xylanase domain, two family 36-like carbohydrate-binding domains CBM36-1 and 2, and a C-terminal CE4 esterase domain. Previous analyses indicated that CBM36-1 deletion slightly increased GH11 catalysis at low pH whereas removal of both CBMs decreased xylanase activity at 60 degrees C from 90 to 56%. Possible cooperativity between the domains suggested by these observations was explored. A crystal structure of the two-domain construct, GH11-CBM36-1, confirmed the structure of the GH11 domain whereas the CBM36-1 domain lacked electron density, possibly indicating a random orientation of the CBM36-1 domain around the GH11 domain. Isothermal titration calorimetry (ITC) experiments similarly did not indicate specific interactions between the individual domains of Xyl supporting a "beads-on-a-string" model for Xyl domains.
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Structural and biophysical characterization of the multidomain xylanase Xyl.,Anye V, Kruger RF, Schubert WD PLoS One. 2022 Jun 3;17(6):e0269188. doi: 10.1371/journal.pone.0269188., eCollection 2022. PMID:35657930<ref>PMID:35657930</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7zsz" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Endo-1,4-beta-xylanase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Anye, V]]
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[[Category: Uncultured bacterium #0087-1D13]]
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[[Category: Schubert, W D]]
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[[Category: Anye V]]
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[[Category: Carbohydrate binding domain]]
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[[Category: Schubert WD]]
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[[Category: Carbohydrate esterase]]
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[[Category: Gh11]]
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[[Category: Hydrolase]]
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[[Category: Interdomain interaction]]
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[[Category: Isothermal titration calorimetry]]
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[[Category: Multidomain protein]]
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Revision as of 06:30, 8 September 2022

Crystal structure of the GH11 domain of a multidomain xylanase from the hindgut metagenome of Trinervitermes trinervoides

PDB ID 7zsz

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