title: Structure of thymidylate kinase from Ehrlichia chaffeensis.
abstract: 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 Å resolution crystal structure of thymidylate kinase from E. chaffeensis in the apo form is presented.
authors: Seattle Structural Genomics Center for Infectious Disease (SSGCID), USA.
authors: David J
authors: DJ
authors: Leibly
authors: Jan
authors: J
authors: Abendroth
authors: Cassie M
authors: CM
authors: Bryan
authors: Banumathi
authors: B
authors: Sankaran
authors: Angela
authors: A
authors: Kelley
authors: Lynn K
authors: LK
authors: Barrett
authors: Lance
authors: L
authors: Stewart
authors: Wesley C
authors: WC
authors: Van Voorhis
mesh_terms: D018360:Crystallography, X-Ray; D018469:Ehrlichia chaffeensis / Q000201:enzymology*; D006801:Humans; D008958:Models, Molecular; D009703:Nucleoside-Phosphate Kinase / Q000737:chemistry*; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D040681:Structural Homology, Protein
chemical_list: D009703:Nucleoside-Phosphate Kinase; C020093:dTMP kinase