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| | ==Structure of cytidine monophosphate kinase from Yersinia pseudotuberculosis== | | ==Structure of cytidine monophosphate kinase from Yersinia pseudotuberculosis== |
| - | <StructureSection load='4e22' size='340' side='right' caption='[[4e22]], [[Resolution|resolution]] 2.32Å' scene=''> | + | <StructureSection load='4e22' size='340' side='right'caption='[[4e22]], [[Resolution|resolution]] 2.32Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4e22]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Yerpy Yerpy]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E22 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4e22]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_pseudotuberculosis_YPIII Yersinia pseudotuberculosis YPIII]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E22 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E22 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cmk, YPK_2669 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=502800 YERPY])</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=4e22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e22 OCA], [https://pdbe.org/4e22 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e22 RCSB], [https://www.ebi.ac.uk/pdbsum/4e22 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e22 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/(d)CMP_kinase (d)CMP kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.25 2.7.4.25] </span></td></tr>
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| - | <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=4e22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e22 OCA], [http://pdbe.org/4e22 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4e22 RCSB], [http://www.ebi.ac.uk/pdbsum/4e22 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4e22 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [[https://www.uniprot.org/uniprot/KCY_YERPY KCY_YERPY]] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Yerpy]] | + | [[Category: Large Structures]] |
| - | [[Category: Acharya, K R]] | + | [[Category: Yersinia pseudotuberculosis YPIII]] |
| - | [[Category: Clark, E A]] | + | [[Category: Acharya KR]] |
| - | [[Category: Cmp/atp binding]] | + | [[Category: Clark EA]] |
| - | [[Category: P-loop]]
| + | |
| - | [[Category: Transferase]]
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| Structural highlights
Function
[KCY_YERPY]
Publication Abstract from PubMed
The need for new antibiotics has become pressing in light of the emergence of antibiotic-resistant strains of human pathogens. Yersinia pestis, the causative agent of plague, is a public health threat and also an agent of concern in biodefence. It is a recently emerged clonal derivative of the enteric pathogen Yersinia pseudotuberculosis. Previously, we developed a bioinformatic approach to identify proteins that may be suitable targets for antimicrobial therapy and in particular for the treatment of plague. One such target was cytidine monophosphate (CMP) kinase, which is an essential gene in some organisms. Previously, we had thought CMP kinase was essential for Y. pseudotuberculosis, but by modification of the mutagenesis approach, we report here the production and characterization of a Deltacmk mutant. The isogenic mutant had a growth defect relative to the parental strain, and was highly attenuated in mice. We have also elucidated the structure of the CMP kinase to 2.32 A, and identified three key residues in the active site that are essential for activity of the enzyme. These findings will have implications for the development of novel CMP kinase inhibitors for therapeutic use.
Structure and function of cytidine monophosphate kinase from Yersinia pseudotuberculosis, essential for virulence but not for survival.,Walker NJ, Clark EA, Ford DC, Bullifent HL, McAlister EV, Duffield ML, Acharya KR, Oyston PC Open Biol. 2012 Dec 5;2(12):120142. doi: 10.1098/rsob.120142. Print 2012. PMID:23271832[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Walker NJ, Clark EA, Ford DC, Bullifent HL, McAlister EV, Duffield ML, Acharya KR, Oyston PC. Structure and function of cytidine monophosphate kinase from Yersinia pseudotuberculosis, essential for virulence but not for survival. Open Biol. 2012 Dec 5;2(12):120142. doi: 10.1098/rsob.120142. Print 2012. PMID:23271832 doi:http://dx.doi.org/10.1098/rsob.120142
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