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==Crystal structure of thymidylate kinase from Ehrlichia chaffeensis at 2.15A resolution== | ==Crystal structure of thymidylate kinase from Ehrlichia chaffeensis at 2.15A resolution== | ||
<StructureSection load='3ld9' size='340' side='right' caption='[[3ld9]], [[Resolution|resolution]] 2.15Å' scene=''> | <StructureSection load='3ld9' size='340' side='right' caption='[[3ld9]], [[Resolution|resolution]] 2.15Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3ld9]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3ld9]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ehrcr Ehrcr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LD9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LD9 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <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"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tmk, ECH_0229 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tmk, ECH_0229 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=205920 EHRCR])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dTMP_kinase dTMP kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.9 2.7.4.9] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dTMP_kinase dTMP kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.9 2.7.4.9] </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=3ld9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ld9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ld9 RCSB], [http://www.ebi.ac.uk/pdbsum/3ld9 PDBsum]</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=3ld9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ld9 OCA], [http://pdbe.org/3ld9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ld9 RCSB], [http://www.ebi.ac.uk/pdbsum/3ld9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ld9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| Line 18: | Line 19: | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ld9 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 28: | Line 29: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3ld9" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Ehrcr]] | ||
[[Category: DTMP kinase]] | [[Category: DTMP kinase]] | ||
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
[[Category: Als collaborative crystallography]] | [[Category: Als collaborative crystallography]] | ||
[[Category: Atp-binding]] | [[Category: Atp-binding]] | ||
[[Category: Ehrlichia chaffeensis]] | |||
[[Category: Emerald biostructure]] | [[Category: Emerald biostructure]] | ||
[[Category: Kinase]] | [[Category: Kinase]] | ||
Revision as of 22:14, 5 August 2016
Crystal structure of thymidylate kinase from Ehrlichia chaffeensis at 2.15A resolutionCrystal structure of thymidylate kinase from Ehrlichia chaffeensis at 2.15A resolution
Structural highlights
Function[KTHY_EHRCR] Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe enzyme thymidylate kinase phosphorylates the substrate thymidine 5'-phosphate (dTMP) to form thymidine 5'-diphosphate (dTDP), which is further phosphorylated to dTTP for incorporation into DNA. Ehrlichia chaffeensis is the etiologic agent of human monocytotropic erlichiosis (HME), a potentially life-threatening tick-borne infection. HME is endemic in the United States from the southern states up to the eastern seaboard. HME is transmitted to humans via the lone star tick Amblyomma americanum. Here, the 2.15 A resolution crystal structure of thymidylate kinase from E. chaffeensis in the apo form is presented. Structure of thymidylate kinase from Ehrlichia chaffeensis.,Leibly DJ, Abendroth J, Bryan CM, Sankaran B, Kelley A, Barrett LK, Stewart L, Van Voorhis WC Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt, 9):1090-4. Epub 2011 Aug 16. PMID:21904055[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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