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| <StructureSection load='3qef' size='340' side='right'caption='[[3qef]], [[Resolution|resolution]] 1.79Å' scene=''> | | <StructureSection load='3qef' size='340' side='right'caption='[[3qef]], [[Resolution|resolution]] 1.79Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3qef]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Celju Celju]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QEF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QEF FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3qef]] 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=3QEF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QEF FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AHR:ALPHA-L-ARABINOFURANOSE'>AHR</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.789Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qed|3qed]], [[3qee|3qee]]</td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AHR:ALPHA-L-ARABINOFURANOSE'>AHR</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gly43N, CJA_3018 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=498211 CELJU])</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=3qef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qef OCA], [https://pdbe.org/3qef PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qef RCSB], [https://www.ebi.ac.uk/pdbsum/3qef PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qef ProSAT]</span></td></tr> |
| <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=3qef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qef OCA], [http://pdbe.org/3qef PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3qef RCSB], [http://www.ebi.ac.uk/pdbsum/3qef PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3qef ProSAT]</span></td></tr> | |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/B3PD60_CELJU B3PD60_CELJU] |
| 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®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 3qef" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Xylosidase|Xylosidase]] | | *[[Xylosidase 3D structures|Xylosidase 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Celju]] | | [[Category: Cellvibrio japonicus Ueda107]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Brumer, H]] | | [[Category: Brumer H]] |
| [[Category: Cartmell, A]] | | [[Category: Cartmell A]] |
| [[Category: Gilbert, H J]] | | [[Category: Gilbert HJ]] |
| [[Category: Larsbrink, J]] | | [[Category: Larsbrink J]] |
| [[Category: Lewis, R J]] | | [[Category: Lewis RJ]] |
| [[Category: Marles-Wright, J]] | | [[Category: Marles-Wright J]] |
| [[Category: Mckee, L S]] | | [[Category: Mckee LS]] |
| [[Category: Pena, M]] | | [[Category: Pena M]] |
| [[Category: Viks-Nielsen, A]] | | [[Category: Viks-Nielsen A]] |
| [[Category: 5-bladed beta propeller]]
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| [[Category: Hydrolase]]
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