3ld9 | pdb_00003ld9

Crystal structure of thymidylate kinase from Ehrlichia chaffeensis at 2.15A resolution

spinqualitylabelsall models 3ld9, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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: EDO, SO4 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Thymidylate kinase 3D structures

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