High-resolution crystal structure of RNA kinase ArK1 from G. acetivorans

被引：0

作者：

Cao, Chulei ^{[1
]}

Zhang, Weizhen ^{[1
]}

Gao, Yanqing ^{[1
]}

Yang, Jie ^{[1
]}

Liu, Hehua ^{[1
]}

Gan, Jianhua ^{[1
]}

机构：

[1] Fudan Univ, Shanghai Sci Tech Inno Ctr Infect & Immun, Collaborat Innovat Ctr Genet & Dev, Sch Life Sci,State Key Lab Genet Engn,Dept Biochem, Shanghai 200438, Peoples R China

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2024年 / 714卷

基金：

中国国家自然科学基金;

关键词：

tRNA modification; U47; phosphorylation; RNA kinase; Ark1; protein; ATP binding; Complex structure; EXTREME THERMOPHILE; PROTEIN-KINASES; RIBOTHYMIDINE; TEMPERATURE; SEQUENCE; ARCHAEA;

D O I：

10.1016/j.bbrc.2024.149966

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

U47 phosphorylation (Up47) is a novel tRNA modification discovered recently; it can confer thermal stability and nuclease resistance to tRNAs. U47 phosphorylation is catalyzed by Archaeal RNA kinase (Ark1) in an ATPdependent manner. However, the structural basis for tRNA and/or ATP binding by Ark1 is unclear. Here, we report the expression, purification, and crystallization studies of Ark1 from G. acetivorans (GaArk1). In addition to the Apo-form structure, one GaArk1-ATP complex was also determined in atomic resolution and revealed the detailed basis for ATP binding by GaArk1. The GaArk1-ATP complex represents the only ATP-bound structure of the Ark1 protein. The majority of the ATP-binding residues are conserved, suggesting that GaArk1 and the homologous proteins share similar mechanism in ATP binding. Sequence and structural analysis further indicated that endogenous guanosine will only inhibit the activities of certain Ark1 proteins, such as Ark1 from T. kodakarensis.

引用

页数：6

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