6k63

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<StructureSection load='6k63' size='340' side='right'caption='[[6k63]], [[Resolution|resolution]] 2.07&Aring;' scene=''>
<StructureSection load='6k63' size='340' side='right'caption='[[6k63]], [[Resolution|resolution]] 2.07&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6k63]] is a 4 chain structure. 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>
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<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>
</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='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>
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<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='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='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'>[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>
<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>
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== 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]
[[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]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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<ref>PMID:31495495</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6k63" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Cytidine deaminase]]
[[Category: Cytidine deaminase]]
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[[Category: Klep7]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Chen, Y]]
[[Category: Chen, Y]]

Revision as of 04:37, 13 February 2020

The crystal structure of cytidine deaminase from Klebsiella pneumoniae

PDB ID 6k63

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