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| | <StructureSection load='6k63' size='340' side='right'caption='[[6k63]], [[Resolution|resolution]] 2.07Å' scene=''> | | <StructureSection load='6k63' size='340' side='right'caption='[[6k63]], [[Resolution|resolution]] 2.07Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6k63]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Klep7 Klep7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K63 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6K63 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6k63]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae_subsp._pneumoniae_MGH_78578 Klebsiella pneumoniae subsp. pneumoniae MGH 78578]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K63 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6K63 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.073Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cdd ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272620 KLEP7])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cytidine_deaminase Cytidine deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.5 3.5.4.5] </span></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=6k63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k63 OCA], [https://pdbe.org/6k63 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6k63 RCSB], [https://www.ebi.ac.uk/pdbsum/6k63 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6k63 ProSAT]</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=6k63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k63 OCA], [http://pdbe.org/6k63 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k63 RCSB], [http://www.ebi.ac.uk/pdbsum/6k63 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k63 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CDD_KLEP7 CDD_KLEP7]] This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.[HAMAP-Rule:MF_01558] | + | [https://www.uniprot.org/uniprot/CDD_KLEP7 CDD_KLEP7] This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.[HAMAP-Rule:MF_01558] |
| | <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 6k63" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6k63" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Deaminase 3D structures|Deaminase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cytidine deaminase]] | + | [[Category: Klebsiella pneumoniae subsp. pneumoniae MGH 78578]] |
| - | [[Category: Klep7]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chen, Y]] | + | [[Category: Chen Y]] |
| - | [[Category: Lan, J]] | + | [[Category: Lan J]] |
| - | [[Category: Liu, W]] | + | [[Category: Liu W]] |
| - | [[Category: Shang, F]] | + | [[Category: Shang F]] |
| - | [[Category: Wang, L]] | + | [[Category: Wang L]] |
| - | [[Category: Xu, Y]] | + | [[Category: Xu Y]] |
| - | [[Category: Cda]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Klebsiella pneumoniae]]
| + | |
| Structural highlights
Function
CDD_KLEP7 This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.[HAMAP-Rule:MF_01558]
Publication Abstract from PubMed
The emergence of drug-resistant strains of Klebsiella pneumoniae, has exacerbated the treatment and control of the disease caused by this bacterium. Cytidine deaminases (CDA) are zinc-dependent enzymes involved in the pyrimidine salvage pathway and catalyze the formation of uridine and deoxyuridine from cytidine and deoxycytidine, respectively. To illustrate the structural basis of CDA for a deeper knowledge of the molecular mechanisms underlying the salvage pathway, we reported here the biochemical and structural analysis of CDA from pathogenic K. pneumonia. KpCDA showed deaminase activity against cytidine as well as its analog cytarabine. The deaminase activity of KpCDA on cytarabine was 1.8 times higher than that on cytidine. KpCDA is composed of an N-terminal catalytic domain and a C-terminal noncatalytic domain. Zinc, which is involved in the activity of the catalytic domain, is coordinated by His102, Cys129, and Cys132, and two 1,4-dioxane molecules were present at the active sites. KpCDA exists as a dimer and shows distinct dimeric interface compared with other CDAs. Our results provide the structural features of KpCDA, and KpCDA might be a potential antibacterial target for the disease caused by K. pneumoniae.
Biochemical and structural analysis of the Klebsiella pneumoniae cytidine deaminase CDA.,Liu W, Shang F, Chen Y, Lan J, Wang L, Chen J, Gao P, Ha NC, Quan C, Nam KH, Xu Y Biochem Biophys Res Commun. 2019 Nov 5;519(2):280-286. doi:, 10.1016/j.bbrc.2019.08.167. Epub 2019 Sep 5. PMID:31495495[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Liu W, Shang F, Chen Y, Lan J, Wang L, Chen J, Gao P, Ha NC, Quan C, Nam KH, Xu Y. Biochemical and structural analysis of the Klebsiella pneumoniae cytidine deaminase CDA. Biochem Biophys Res Commun. 2019 Nov 5;519(2):280-286. doi:, 10.1016/j.bbrc.2019.08.167. Epub 2019 Sep 5. PMID:31495495 doi:http://dx.doi.org/10.1016/j.bbrc.2019.08.167
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