Structure of thymidylate kinase from Ehrlichia chaffeensis

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

doi:10.1107/s174430911101493x

Structure of thymidylate kinase from Ehrlichia chaffeensis

Journal Article · Tue Aug 16 00:00:00 EDT 2011 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/s174430911101493x· OSTI ID:1625810

Leibly, David J. ^[1]; Abendroth, Jan ^[2]; Bryan, Cassie M. ^[3]; Sankaran, Banumathi ^[4]; Kelley, Angela ^[5]; Barrett, Lynn K. ^[5]; Stewart, Lance ^[2]; Van Voorhis, Wesley C. ^[5]

Seattle Structural Genomics Center for Infectious Disease (SSGCID), Seattle, WA (United States); Univ. of Washington, Seattle, WA (United States). School of Medicine. Dept. of Allergy and Infectious Diseases; DOE/OSTI
Seattle Structural Genomics Center for Infectious Disease (SSGCID), Seattle, WA (United States); Emerald BioStructures Inc., Bainbridge Island, WA (United States)
Seattle Structural Genomics Center for Infectious Disease (SSGCID), Seattle, WA (United States); Univ. of Washington, Seattle, WA (United States). School of Medicine. Dept. of Allergy and Infectious Diseases
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Berkeley Center for Structural Biology
Seattle Structural Genomics Center for Infectious Disease (SSGCID), Seattle, WA (United States); Univ. of Washington, Seattle, WA (United States). School of Medicine. Dept. of Allergy and Infectious Diseases

The enzyme thymidylate kinase phosphorylates the substrate thymidine 50 -phosphate (dTMP) to form thymidine 50 -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.

View Accepted Manuscript (DOE)

Research Organization:: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)

Sponsoring Organization:: National Institute of Allergy and Infectious Diseases (NIAID); National Institutes of Health (NIH); USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division

Grant/Contract Number:: AC02-05CH11231

OSTI ID:: 1625810

Journal Information:: Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: 9 Vol. 67; ISSN ACSFCL; ISSN 1744-3091

Publisher:: International Union of CrystallographyCopyright Statement

Country of Publication:: United States

Language:: English

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Related Subjects

59 BASIC BIOLOGICAL SCIENCES
Ehrlichia chaffeensis
biochemistry & molecular biology
biophysics
crystallography
human monocytotropic erlichiosis
thymidine 5′-diphosphate
thymidine 5′-phosphate
thymidylate kinases.

Structure of thymidylate kinase from Ehrlichia chaffeensis

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References (24)

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