3w6f: Difference between revisions
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<StructureSection load='3w6f' size='340' side='right'caption='[[3w6f]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='3w6f' size='340' side='right'caption='[[3w6f]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3w6f]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3w6f]] 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=3W6F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W6F FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3w6b|3w6b]], [[3w6c|3w6c]], [[3w6d|3w6d]], [[3w6e|3w6e]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3w6b|3w6b]], [[3w6c|3w6c]], [[3w6d|3w6d]], [[3w6e|3w6e]]</div></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Chitinase Chitinase], with EC number [https://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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3w6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w6f OCA], [https://pdbe.org/3w6f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w6f RCSB], [https://www.ebi.ac.uk/pdbsum/3w6f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w6f ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Revision as of 08:24, 3 August 2022
Crystal structure of catalytic domain of chitinase from Ralstonia sp. A-471 (E162Q) in complex with disaccharideCrystal structure of catalytic domain of chitinase from Ralstonia sp. A-471 (E162Q) in complex with disaccharide
Structural highlights
Publication Abstract from PubMedChitinase 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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