3qee

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<StructureSection load='3qee' size='340' side='right'caption='[[3qee]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
<StructureSection load='3qee' size='340' side='right'caption='[[3qee]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3qee]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Celju Celju]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QEE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QEE FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3qee]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cellvibrio_japonicus_Ueda107 Cellvibrio japonicus Ueda107]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QEE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QEE FirstGlance]. <br>
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</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=CA:CALCIUM+ION'>CA</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]] 1.64&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3qed|3qed]], [[3qef|3qef]]</div></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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gly43N, CJA_3018 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=498211 CELJU])</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=3qee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qee OCA], [https://pdbe.org/3qee PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qee RCSB], [https://www.ebi.ac.uk/pdbsum/3qee PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qee 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=3qee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qee OCA], [https://pdbe.org/3qee PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qee RCSB], [https://www.ebi.ac.uk/pdbsum/3qee PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qee 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/B3PD60_CELJU B3PD60_CELJU]
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Reflecting the diverse chemistry of plant cell walls, microorganisms that degrade these composite structures synthesize an array of glycoside hydrolases. These enzymes are organized into sequence-, mechanism- and structure-based families. Genomic data has shown that several organisms that degrade the plant cell wall contain a large number of genes encoding family 43 (GH43) glycoside hydrolases. Here we report the biochemical properties of the GH43 enzymes of a saprophytic soil bacterium, Cellvibrio japonicus, and a human colonic symbiont, Bacteroides thetaiotaomicron. The data show that C. japonicus uses predominantly exo-acting enzymes to degrade arabinan into arabinose, while B. thetaiotaomicron deploys a combination of endo and side chain-cleaving glycoside hydrolases. Both organisms, however, utilize an arabinan-specific alpha-1,2-arabinofuranosidase in the degradative process, an activity that has not previously been reported. The enzyme can cleave alpha-1,2-arabinofuranose decorations in single or double substitutions, the latter being recalcitrant to the action of other arabinofuranosidases. The crystal structure of the C. japonicus arabinan-specific alpha-1,2-arabinofuranosidase, CjAbf43A displays a 5-bladed beta-propeller fold. The specificity of the enzyme for arabinan is conferred by a surface cleft that is complementary to the helical backbone of the polysaccharide. The specificity of CjAbf43A for alpha-1,2-L-arabinofuranose side chains is conferred by a polar residue that orientates the arabinan backbone such that O2 arabinose decorations are directed into the active site pocket. A shelf-like structure adjacent to the active site pocket accommodates O3 arabinose side chains, explaining how the enzyme can target O2 linkages that are components of single or double substitutions.
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The structure and function of an arabinan-specific alpha-1,2-arabinofuranosidase identified from screening the activities of bacterial GH43 glycoside hydrolases.,Cartmell A, McKee L, Pena MJ, Larsbrink J, Brumer H, Kaneko S, Ichinose H, Lewis RJ, Vikso-Nielsen A, Gilbert HJ, Marles-Wright J J Biol Chem. 2011 Feb 21. PMID:21339299<ref>PMID:21339299</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 3qee" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Xylosidase 3D structures|Xylosidase 3D structures]]
*[[Xylosidase 3D structures|Xylosidase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Celju]]
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[[Category: Cellvibrio japonicus Ueda107]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Brumer, H]]
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[[Category: Brumer H]]
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[[Category: Cartmell, A]]
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[[Category: Cartmell A]]
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[[Category: Gilbert, H J]]
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[[Category: Gilbert HJ]]
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[[Category: Larsbrink, J]]
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[[Category: Larsbrink J]]
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[[Category: Lewis, R J]]
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[[Category: Lewis RJ]]
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[[Category: Marles-Wright, J]]
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[[Category: Marles-Wright J]]
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[[Category: Mckee, L S]]
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[[Category: Mckee LS]]
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[[Category: Pena, M]]
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[[Category: Pena M]]
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[[Category: Viks-Nielsen, A]]
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[[Category: Viks-Nielsen A]]
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[[Category: 5-bladed beta propeller]]
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[[Category: Hydrolase]]
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Current revision

The structure and function of an arabinan-specific alpha-1,2-arabinofuranosidase identified from screening the activities of bacterial GH43 glycoside hydrolases

PDB ID 3qee

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