View source for 5bza


==Crystal structure of CbsA from Thermotoga neapolitana==
<StructureSection load='5bza' size='340' side='right'caption='[[5bza]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5bza]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_neapolitana Thermotoga neapolitana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BZA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BZA 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]] 2.002&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</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=5bza FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bza OCA], [https://pdbe.org/5bza PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bza RCSB], [https://www.ebi.ac.uk/pdbsum/5bza PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bza ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9AG27_THENE Q9AG27_THENE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
CbsA from the thermophilic marine bacteria Thermotoga neapolitana is a chitinolyitc enzyme that can cleave a glycosidic bond of the polymer N-acetylglucosamine at the non-reducing end. This enzyme has particularly high activity on di-N-acetylchitobiose. CbsA consists of a family of 3 glycoside hydrolase (GH3)-type catalytic domains and a unique C-terminal domain. The C-terminal domain distinguishes CbsA from other GH3-type enzymes. Sequence analyses have suggested that CbsA has the Asp-His dyad as a general acid/base with the NagZ of Bacillus subtilis and the Salmonella enterica serovar Typhimurium. Here, we determined the crystal structure of CbsA from T. neapolitana at a resolution of 2.0 A using the Zn-SAD method, revealing a unique homodimeric assembly facilitated by the C-terminal domains in the dimer. We observed that CbsA is strongly inhibited by ZnCl2, and two zinc ions were consistently bound in the active site. Our results can explain the zinc ion's inhibition mechanism in the subfamily of GH3 enzymes, and provide information on the structural diversity and substrate specificity of this hydrolase family.

Crystal structure of beta-N-acetylglucosaminidase CbsA from Thermotoga neapolitana.,Kim JS, Yoon BY, Ahn J, Cha J, Ha NC Biochem Biophys Res Commun. 2015 Aug 28;464(3):869-74. doi:, 10.1016/j.bbrc.2015.07.053. Epub 2015 Jul 14. PMID:26187666<ref>PMID:26187666</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5bza" style="background-color:#fffaf0;"></div>

==See Also==
*[[Beta-N-acetylhexosaminidase 3D structures|Beta-N-acetylhexosaminidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermotoga neapolitana]]
[[Category: Ha NC]]
[[Category: Kim JS]]
[[Category: Yoon BY]]