3LD9
Crystal structure of thymidylate kinase from Ehrlichia chaffeensis at 2.15A resolution
Summary for 3LD9
| Entry DOI | 10.2210/pdb3ld9/pdb |
| Descriptor | Thymidylate kinase, SULFATE ION, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | ssgcid, nih, niaid, sbri, uw, emerald biostructures, ehrlichia chaffeensis, thymidylate kinase, als collaborative crystallography, atp-binding, kinase, nucleotide biosynthesis, nucleotide-binding, transferase, structural genomics, seattle structural genomics center for infectious disease |
| Biological source | Ehrlichia chaffeensis |
| Total number of polymer chains | 4 |
| Total formula weight | 102560.75 |
| Authors | Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2010-01-12, release date: 2010-02-16, Last modification date: 2023-09-06) |
| Primary citation | Leibly, D.J.,Abendroth, J.,Bryan, C.M.,Sankaran, B.,Kelley, A.,Barrett, L.K.,Stewart, L.,Van Voorhis, W.C. Structure of thymidylate kinase from Ehrlichia chaffeensis. Acta Crystallogr.,Sect.F, 67:1090-1094, 2011 Cited by PubMed 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. PubMed: 21904055DOI: 10.1107/S174430911101493X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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