3ld9
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
FunctionKTHY_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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