3LD9

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

3LD9 の概要

• エントリーDOI: 10.2210/pdb3ld9/pdb
• 分子名称: Thymidylate kinase, SULFATE ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: 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
• 由来する生物種: Ehrlichia chaffeensis
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 102560.75

構造登録者

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (登録日: 2010-01-12, 公開日: 2010-02-16, 最終更新日: 2023-09-06)

主引用文献

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

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: 21904055
DOI: 10.1107/S174430911101493X

実験手法

X-RAY DIFFRACTION (2.15 Å)