Structure of thymidylate kinase from Ehrlichia chaffeensis.

David J Leibly, Jan Abendroth, Cassie M Bryan, Banumathi Sankaran, Angela Kelley, Lynn K Barrett, Lance Stewart, Wesley C Van Voorhis

Seattle Structural Genomics Center for Infectious Disease (SSGCID), USA.

Acta crystallographica. Section F, Structural biology and crystallization communications 2011 Sep 1

filter terms:

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.

Citation

David J Leibly, Jan Abendroth, Cassie M Bryan, Banumathi Sankaran, Angela Kelley, Lynn K Barrett, Lance Stewart, Wesley C Van Voorhis. Structure of thymidylate kinase from Ehrlichia chaffeensis. Acta crystallographica. Section F, Structural biology and crystallization communications. 2011 Sep 1;67(Pt 9):1090-4