5msx

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==Glycoside hydrolase BT_3662==
==Glycoside hydrolase BT_3662==
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<StructureSection load='5msx' size='340' side='right' caption='[[5msx]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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<StructureSection load='5msx' size='340' side='right'caption='[[5msx]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5msx]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MSX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MSX FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5msx]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_thetaiotaomicron_VPI-5482 Bacteroides thetaiotaomicron VPI-5482]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MSX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MSX FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=144:TRIS-HYDROXYMETHYL-METHYL-AMMONIUM'>144</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene></td></tr>
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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]] 2.1&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5msx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5msx OCA], [http://pdbe.org/5msx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5msx RCSB], [http://www.ebi.ac.uk/pdbsum/5msx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5msx ProSAT]</span></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=144:TRIS-HYDROXYMETHYL-METHYL-AMMONIUM'>144</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</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=5msx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5msx OCA], [https://pdbe.org/5msx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5msx RCSB], [https://www.ebi.ac.uk/pdbsum/5msx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5msx ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q8A1J9_BACTN Q8A1J9_BACTN]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The metabolism of carbohydrate polymers drives microbial diversity in the human gut microbiota. It is unclear, however, whether bacterial consortia or single organisms are required to depolymerize highly complex glycans. Here we show that the gut bacterium Bacteroides thetaiotaomicron uses the most structurally complex glycan known: the plant pectic polysaccharide rhamnogalacturonan-II, cleaving all but 1 of its 21 distinct glycosidic linkages. The deconstruction of rhamnogalacturonan-II side chains and backbone are coordinated to overcome steric constraints, and the degradation involves previously undiscovered enzyme families and catalytic activities. The degradation system informs revision of the current structural model of rhamnogalacturonan-II and highlights how individual gut bacteria orchestrate manifold enzymes to metabolize the most challenging glycan in the human diet.
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Complex pectin metabolism by gut bacteria reveals novel catalytic functions.,Ndeh D, Rogowski A, Cartmell A, Luis AS, Basle A, Gray J, Venditto I, Briggs J, Zhang X, Labourel A, Terrapon N, Buffetto F, Nepogodiev S, Xiao Y, Field RA, Zhu Y, O'Neill MA, Urbanowicz BR, York WS, Davies GJ, Abbott DW, Ralet MC, Martens EC, Henrissat B, Gilbert HJ Nature. 2017 Mar 22. doi: 10.1038/nature21725. PMID:28329766<ref>PMID:28329766</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 5msx" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Basle, A]]
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[[Category: Bacteroides thetaiotaomicron VPI-5482]]
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[[Category: Cartmell, A]]
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[[Category: Large Structures]]
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[[Category: Gilbert, H J]]
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[[Category: Basle A]]
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[[Category: Labourel, A]]
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[[Category: Cartmell A]]
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[[Category: Luis, A S]]
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[[Category: Gilbert HJ]]
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[[Category: Ndeh, D]]
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[[Category: Labourel A]]
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[[Category: Rogowski, A]]
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[[Category: Luis AS]]
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[[Category: Venditto, I]]
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[[Category: Ndeh D]]
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[[Category: Arabinofuranosidase]]
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[[Category: Rogowski A]]
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[[Category: Gh43]]
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[[Category: Venditto I]]
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[[Category: Glycoside hydrolase]]
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[[Category: Hydrolase]]
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[[Category: Plant pectin]]
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[[Category: Rgii]]
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Current revision

Glycoside hydrolase BT_3662

PDB ID 5msx

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