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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]] 2.15&Aring;' scene=''>
<StructureSection load='3ld9' size='340' side='right'caption='[[3ld9]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<table><tr><td colspan='2'>[[3ld9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Ehrlichia_chaffeensis_str._Arkansas Ehrlichia chaffeensis str. Arkansas]. 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 [https://proteopedia.org/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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</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=205920 EHRCR])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=3ld9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ld9 OCA], [https://pdbe.org/3ld9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ld9 RCSB], [https://www.ebi.ac.uk/pdbsum/3ld9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ld9 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=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 ==
[[http://www.uniprot.org/uniprot/KTHY_EHRCR KTHY_EHRCR]] Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis (By similarity).  
[https://www.uniprot.org/uniprot/KTHY_EHRCR KTHY_EHRCR] Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ld/3ld9_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ld/3ld9_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
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==See Also==
==See Also==
*[[Thymidylate kinase|Thymidylate kinase]]
*[[Thymidylate kinase 3D structures|Thymidylate kinase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ehrcr]]
[[Category: Ehrlichia chaffeensis str. Arkansas]]
[[Category: DTMP kinase]]
[[Category: Large Structures]]
[[Category: Structural genomic]]
[[Category: Als collaborative crystallography]]
[[Category: Atp-binding]]
[[Category: Ehrlichia chaffeensis]]
[[Category: Emerald biostructure]]
[[Category: Kinase]]
[[Category: Niaid]]
[[Category: Nih]]
[[Category: Nucleotide biosynthesis]]
[[Category: Nucleotide-binding]]
[[Category: Sbri]]
[[Category: Ssgcid]]
[[Category: Thymidylate kinase]]
[[Category: Transferase]]
[[Category: Uw]]

Latest revision as of 11:35, 6 September 2023

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

3ld9 is a 4 chain structure with sequence from Ehrlichia chaffeensis str. Arkansas. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.15Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

The 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 Also

References

  1. Leibly DJ, Abendroth J, Bryan CM, Sankaran B, Kelley A, Barrett LK, Stewart L, Van Voorhis WC. Structure of thymidylate kinase from Ehrlichia chaffeensis. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt, 9):1090-4. Epub 2011 Aug 16. PMID:21904055 doi:10.1107/S174430911101493X

3ld9, resolution 2.15Å

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OCA