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==Crystal structure of catalytic domain of chitinase from Ralstonia sp. A-471 in complex with disaccharide== | |||
<StructureSection load='3w6c' size='340' side='right' caption='[[3w6c]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3w6c]] 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=3W6C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3W6C 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> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3w6b|3w6b]], [[3w6d|3w6d]], [[3w6e|3w6e]], [[3w6f|3w6f]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3w6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w6c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3w6c RCSB], [http://www.ebi.ac.uk/pdbsum/3w6c PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
==See Also== | |||
*[[Chitinase|Chitinase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Chitinase]] | [[Category: Chitinase]] | ||
[[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]] | [[Category: Enzyme]] | ||
[[Category: Gh family 23]] | [[Category: Gh family 23]] | ||
[[Category: Glycoside hydrolase]] | [[Category: Glycoside hydrolase]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
Revision as of 10:02, 21 December 2014
Crystal structure of catalytic domain of chitinase from Ralstonia sp. A-471 in complex with disaccharideCrystal structure of catalytic domain of chitinase from Ralstonia sp. A-471 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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