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| <StructureSection load='3w6b' size='340' side='right'caption='[[3w6b]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='3w6b' size='340' side='right'caption='[[3w6b]], [[Resolution|resolution]] 1.90Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3w6b]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ralstonia_sp._a-471 Ralstonia sp. a-471]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W6B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3W6B FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3w6b]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Ralstonia_sp._A-471 Ralstonia sp. A-471]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W6B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W6B FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.9Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3w6c|3w6c]], [[3w6d|3w6d]], [[3w6e|3w6e]], [[3w6f|3w6f]]</td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chitinase Chitinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.14 3.2.1.14] </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=3w6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w6b OCA], [https://pdbe.org/3w6b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w6b RCSB], [https://www.ebi.ac.uk/pdbsum/3w6b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w6b 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=3w6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w6b OCA], [http://pdbe.org/3w6b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3w6b RCSB], [http://www.ebi.ac.uk/pdbsum/3w6b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3w6b ProSAT]</span></td></tr> | |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/B7XCV4_9RALS B7XCV4_9RALS] |
| Chitinase C from Ralstonia sp. A-471 (Ra-ChiC) has a catalytic domain sequence similar to goose-type (G-type) lysozymes and, unlike other chitinases, belongs to glycohydrolase (GH) family 23. Using NMR spectroscopy, however, Ra-ChiC was found to interact only with the chitin dimer but not with the peptidoglycan fragment. Here we report the crystal structures of wild-type, E141Q, and E162Q of the catalytic domain of Ra-ChiC with or without chitin oligosaccharides. Ra-ChiC has a substrate-binding site including a tunnel-shaped cavity, which determines the substrate specificity. Mutation analyses based on this structural information indicated that a highly conserved Glu-141 acts as a catalytic acid, and that Asp-226 located at the roof of the tunnel activates a water molecule as a catalytic base. The unique arrangement of the catalytic residues makes a clear contrast to the other GH23 members and also to inverting GH19 chitinases.
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| Crystal Structures of the Catalytic Domain of a Novel Glycohydrolase Family 23 Chitinase from Ralstonia sp. A-471 Reveals a Unique Arrangement of the Catalytic Residues for Inverting Chitin Hydrolysis.,Arimori T, Kawamoto N, Shinya S, Okazaki N, Nakazawa M, Miyatake K, Fukamizo T, Ueda M, Tamada T J Biol Chem. 2013 Jun 28;288(26):18696-706. doi: 10.1074/jbc.M113.462135. Epub, 2013 May 8. PMID:23658014<ref>PMID:23658014</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 3w6b" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Chitinase 3D structures|Chitinase 3D structures]] | | *[[Chitinase 3D structures|Chitinase 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Chitinase]]
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| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Ralstonia sp. a-471]] | | [[Category: Ralstonia sp. A-471]] |
| [[Category: Arimori, T]] | | [[Category: Arimori T]] |
| [[Category: Fukamizo, T]] | | [[Category: Fukamizo T]] |
| [[Category: Kawamoto, N]] | | [[Category: Kawamoto N]] |
| [[Category: Miyatake, K]] | | [[Category: Miyatake K]] |
| [[Category: Nakazawa, M]] | | [[Category: Nakazawa M]] |
| [[Category: Okazaki, N]] | | [[Category: Okazaki N]] |
| [[Category: Tamada, T]] | | [[Category: Tamada T]] |
| [[Category: Ueda, M]] | | [[Category: Ueda M]] |
| [[Category: Enzyme]]
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| [[Category: Gh family 23]]
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| [[Category: Glycoside hydrolase]]
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| [[Category: Hydrolase]]
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