4e22: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
[[ | ==Structure of cytidine monophosphate kinase from Yersinia pseudotuberculosis== | ||
<StructureSection load='4e22' size='340' side='right' caption='[[4e22]], [[Resolution|resolution]] 2.32Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4e22]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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> | |||
<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 Yersinia pseudotuberculosis YPIII])</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> | |||
<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://www.rcsb.org/pdb/explore.do?structureId=4e22 RCSB], [http://www.ebi.ac.uk/pdbsum/4e22 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:23271832</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | |||
*[[Cytidine monophosphate kinase|Cytidine monophosphate kinase]] | |||
== | == References == | ||
[[ | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Yersinia pseudotuberculosis ypiii]] | [[Category: Yersinia pseudotuberculosis ypiii]] | ||
[[Category: Acharya, K R | [[Category: Acharya, K R]] | ||
[[Category: Clark, E A | [[Category: Clark, E A]] | ||
[[Category: Cmp/atp binding]] | [[Category: Cmp/atp binding]] | ||
[[Category: P-loop]] | [[Category: P-loop]] | ||
[[Category: Transferase]] | [[Category: Transferase]] |
Revision as of 17:28, 9 December 2014
Structure of cytidine monophosphate kinase from Yersinia pseudotuberculosisStructure of cytidine monophosphate kinase from Yersinia pseudotuberculosis
Structural highlights
Publication Abstract from PubMedThe 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 AlsoReferences
|
|