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'''Unreleased structure'''


The entry 4ny2 is ON HOLD
==Structure of Vibrio cholerae chitin de-N-acetylase in complex with acetate ion (ACT) in P 21==
<StructureSection load='4ny2' size='340' side='right'caption='[[4ny2]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ny2]] 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=4NY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NY2 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.879&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4ny2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ny2 OCA], [https://pdbe.org/4ny2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ny2 RCSB], [https://www.ebi.ac.uk/pdbsum/4ny2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ny2 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== 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.


Authors: Albesa-Jove, D., Andres, E., Biarnes, X., Planas, A., Guerin, M.E.
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<ref>PMID:24810719</ref>


Description: Vibrio cholerae protein
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ny2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vibrio cholerae O1 str. NHCC-010F]]
[[Category: Albesa-Jove D]]
[[Category: Andres E]]
[[Category: Biarnes X]]
[[Category: Guerin ME]]
[[Category: Planas A]]
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