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| | <StructureSection load='4oui' size='340' side='right'caption='[[4oui]], [[Resolution|resolution]] 2.17Å' scene=''> | | <StructureSection load='4oui' size='340' side='right'caption='[[4oui]], [[Resolution|resolution]] 2.17Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4oui]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibrio_cholerae_o1_str._nhcc-010f Vibrio cholerae o1 str. nhcc-010f]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OUI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OUI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4oui]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae_O1_str._NHCC-010F Vibrio cholerae O1 str. NHCC-010F]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OUI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OUI FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CTO:TRIACETYLCHITOTRIOSE'>CTO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900017:triacetyl-beta-chitotriose'>PRD_900017</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ny2|4ny2]], [[4nz5|4nz5]], [[4nz4|4nz4]], [[4nz3|4nz3]], [[4nz1|4nz1]], [[4nyy|4nyy]], [[4nyu|4nyu]]</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=4oui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oui OCA], [https://pdbe.org/4oui PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oui RCSB], [https://www.ebi.ac.uk/pdbsum/4oui PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oui ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VCNHCC010F_001593 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1095658 Vibrio cholerae O1 str. NHCC-010F])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chitin_deacetylase Chitin deacetylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.41 3.5.1.41] </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=4oui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oui OCA], [http://pdbe.org/4oui PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4oui RCSB], [http://www.ebi.ac.uk/pdbsum/4oui PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4oui ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chitin deacetylase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Vibrio cholerae o1 str. nhcc-010f]] | + | [[Category: Vibrio cholerae O1 str. NHCC-010F]] |
| - | [[Category: Albesa-Jove, D]] | + | [[Category: Albesa-Jove D]] |
| - | [[Category: Andres, E]] | + | [[Category: Andres E]] |
| - | [[Category: Biarnes, X]] | + | [[Category: Biarnes X]] |
| - | [[Category: Guerin, M E]] | + | [[Category: Guerin ME]] |
| - | [[Category: Planas, A]] | + | [[Category: Planas A]] |
| - | [[Category: Carbohydrate esterase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Publication Abstract from PubMed
Cell signaling and other biological activities of chitooligosaccharides (COSs) seem to be dependent not only on the degree of polymerization, but markedly on the specific de-N-acetylation pattern. Chitin de-N-acetylases (CDAs) catalyze the hydrolysis of the acetamido group in GlcNAc residues of chitin, chitosan, and COS. A major challenge is to understand how CDAs specifically define the distribution of GlcNAc and GlcNH2 moieties in the oligomeric chain. We report the crystal structure of the Vibrio cholerae CDA in four relevant states of its catalytic cycle. The two enzyme complexes with chitobiose and chitotriose represent the first 3D structures of a CDA with its natural substrates in a productive mode for catalysis, thereby unraveling an induced-fit mechanism with a significant conformational change of a loop closing the active site. We propose that the deacetylation pattern exhibited by different CDAs is governed by critical loops that shape and differentially block accessible subsites in the binding cleft of CE4 enzymes.
Structural basis of chitin oligosaccharide deacetylation.,Andres E, Albesa-Jove D, Biarnes X, Moerschbacher BM, Guerin ME, Planas A Angew Chem Int Ed Engl. 2014 Jul 1;53(27):6882-7. doi: 10.1002/anie.201400220., Epub 2014 May 8. PMID:24810719[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Andres E, Albesa-Jove D, Biarnes X, Moerschbacher BM, Guerin ME, Planas A. Structural basis of chitin oligosaccharide deacetylation. Angew Chem Int Ed Engl. 2014 Jul 1;53(27):6882-7. doi: 10.1002/anie.201400220., Epub 2014 May 8. PMID:24810719 doi:http://dx.doi.org/10.1002/anie.201400220
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