8va4

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Current revision (07:10, 23 October 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 8va4 is ON HOLD until Paper Publication
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==Crystal structure of CapGH16_3 enzyme retrieved from capybara gut metagenome==
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<StructureSection load='8va4' size='340' side='right'caption='[[8va4]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8va4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Metagenome Metagenome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8VA4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8VA4 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.96&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8va4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8va4 OCA], [https://pdbe.org/8va4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8va4 RCSB], [https://www.ebi.ac.uk/pdbsum/8va4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8va4 ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Gut microbiota members from the Bacteroidota phylum play a pivotal role in mammalian health and metabolism. They thrive in this diverse ecosystem due to their notable ability to cope with distinct recalcitrant dietary glycans via polysaccharide utilization loci (PULs). Our study reveals that a PUL from an herbivore gut bacterium belonging to the Bacteroidota phylum, with a gene composition similar to that in the human gut, exhibits extended functionality. While the human gut PUL targets mixed-linkage beta-glucans specifically, the herbivore gut PUL also efficiently processes linear and substituted beta-1,3-glucans. This gain of function emerges from molecular adaptations in recognition proteins and carbohydrate-active enzymes, including a beta-glucosidase specialized for beta(1,6)-glucosyl linkages, a typical substitution in beta(1,3)-glucans. These findings broaden the existing model for non-cellulosic beta-glucans utilization by gut bacteria, revealing an additional layer of functional and evolutionary complexity within the gut microbiota, beyond conventional gene insertions/deletions to intricate biochemical interactions.
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Authors:
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A functionally augmented carbohydrate utilization locus from herbivore gut microbiota fueled by dietary beta-glucans.,Mandelli F, Martins MP, Chinaglia M, Lima EA, Morais MAB, Lima TB, Cabral L, Pirolla RAS, Fuzita FJ, Paixao DAA, Andrade MO, Wolf LD, Vieira PS, Persinoti GF, Murakami MT NPJ Biofilms Microbiomes. 2024 Oct 14;10(1):105. doi: 10.1038/s41522-024-00578-6. PMID:39397008<ref>PMID:39397008</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 8va4" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Metagenome]]
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[[Category: Chinaglia M]]
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[[Category: Lima EA]]
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[[Category: Mandelli F]]
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[[Category: Martins MP]]
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[[Category: Morais MAB]]
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[[Category: Murakami MT]]
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[[Category: Vieira PS]]

Current revision

Crystal structure of CapGH16_3 enzyme retrieved from capybara gut metagenome

PDB ID 8va4

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