3wx7: Difference between revisions
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==Crystal structure of COD== | |||
<StructureSection load='3wx7' size='340' side='right'caption='[[3wx7]], [[Resolution|resolution]] 1.35Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3wx7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_parahaemolyticus Vibrio parahaemolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WX7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WX7 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]] 1.349Å</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=3wx7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wx7 OCA], [https://pdbe.org/3wx7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wx7 RCSB], [https://www.ebi.ac.uk/pdbsum/3wx7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wx7 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A6P4T5_VIBPH A6P4T5_VIBPH] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The X-ray crystal structure of chitin oligosaccharide deacetylase from Vibrio parahaemolyticus (Vp-COD) was determined at an 1.35 A resolution. The amino acid sequence and structure of Vp-COD show that the enzyme comprises one polysaccharide deacetylase domain (PDD) and two carbohydrate-binding domains (CBDs). On the basis of a chitin-binding assay with Vp-COD and its CBDs-deleted mutant, it was confirmed that CBDs can adhere to chitin. The catalytic activity of the CBDs-deleted mutant was only mildly depressed compared with that of Vp-COD, indicating that CBDs are unlikely to affect the configuration of the active center residues in active site of PDD. | |||
Structure-based analysis of domain function of chitin oligosaccharide deacetylase from Vibrio parahaemolyticus.,Hirano T, Sugiyama K, Sakaki Y, Hakamata W, Park SY, Nishio T FEBS Lett. 2015 Jan 2;589(1):145-51. doi: 10.1016/j.febslet.2014.11.039. Epub, 2014 Dec 3. PMID:25479092<ref>PMID:25479092</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3wx7" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Vibrio parahaemolyticus]] | |||
[[Category: Hirano T]] | |||
[[Category: Nishio T]] | |||
[[Category: Park S-Y]] | |||
[[Category: Sugiyama K]] | |||
