3W8R
Mutant structure of Thermus thermophilus HB8 uridine-cytidine kinase
3W8R の概要
| エントリーDOI | 10.2210/pdb3w8r/pdb |
| 関連するPDBエントリー | 3ASY 3ASZ 3W34 |
| 分子名称 | Uridine kinase, 4-AMINO-1-BETA-D-RIBOFURANOSYL-2(1H)-PYRIMIDINONE, PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER, ... (4 entities in total) |
| 機能のキーワード | kinase, transferase |
| 由来する生物種 | Thermus thermophilus |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 48866.24 |
| 構造登録者 | Tomoike, F.,Nakagawa, N.,Masui, R.,Kuramitsu, S. (登録日: 2013-03-21, 公開日: 2014-03-26, 最終更新日: 2024-03-20) |
| 主引用文献 | Tomoike, F.,Nakagawa, N.,Fukui, K.,Yano, T.,Kuramitsu, S.,Masui, R. Indispensable residue for uridine binding in the uridine-cytidine kinase family. Biochem Biophys Rep, 11:93-98, 2017 Cited by PubMed Abstract: Uridine-cytidine kinase (UCK), including human UCK2, are a family of enzymes that generally phosphorylate both uridine and cytidine. However, UCK of HB8 (ttCK) phosphorylates only cytidine. This cytidine-restricted activity is thought to depend on Tyr93, although the precise mechanism remains unresolved. Exhaustive mutagenesis of Tyr93 in ttCK revealed that the uridine phosphorylation activity was restored only by replacement of Tyr93 with His or Gln. Replacement of His117 in human UCK2, corresponding to residue Tyr93 in ttCK, by Tyr resulted in a loss of uridine phosphorylation activity. These findings indicated that uridine phosphorylation activity commonly depends on a single residue in the UCK family. PubMed: 28955773DOI: 10.1016/j.bbrep.2017.07.002 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.5 Å) |
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