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| | ==Crystal structure of Zn bound CbsA from Thermotoga neapolitana== | | ==Crystal structure of Zn bound CbsA from Thermotoga neapolitana== |
| - | <StructureSection load='5c0q' size='340' side='right' caption='[[5c0q]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='5c0q' size='340' side='right'caption='[[5c0q]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5c0q]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_49049 Atcc 49049]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C0Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C0Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5c0q]] 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=5C0Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C0Q FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5bza|5bza]]</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=5c0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c0q OCA], [https://pdbe.org/5c0q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c0q RCSB], [https://www.ebi.ac.uk/pdbsum/5c0q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c0q ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cbsA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2337 ATCC 49049])</td></tr>
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| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </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=5c0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c0q OCA], [http://pdbe.org/5c0q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c0q RCSB], [http://www.ebi.ac.uk/pdbsum/5c0q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c0q ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9AG27_THENE Q9AG27_THENE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5c0q" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5c0q" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Beta-N-acetylhexosaminidase 3D structures|Beta-N-acetylhexosaminidase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 49049]] | + | [[Category: Large Structures]] |
| - | [[Category: Beta-N-acetylhexosaminidase]] | + | [[Category: Thermotoga neapolitana]] |
| - | [[Category: Ha, N C]] | + | [[Category: Ha NC]] |
| - | [[Category: Kim, J S]] | + | [[Category: Kim JS]] |
| - | [[Category: Yoon, B Y]] | + | [[Category: Yoon BY]] |
| - | [[Category: Beta-n-acetylglucosaminidase]]
| + | |
| - | [[Category: Cbsa]]
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| - | [[Category: Hydrolase]]
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| - | [[Category: Thermostable enzyme]]
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| - | [[Category: Thermotoga]]
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| Structural highlights
Function
Q9AG27_THENE
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kim JS, Yoon BY, Ahn J, Cha J, Ha NC. Crystal structure of beta-N-acetylglucosaminidase CbsA from Thermotoga neapolitana. 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 doi:http://dx.doi.org/10.1016/j.bbrc.2015.07.053
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