1TQP

Crystal Structure of A. fulgidus Rio2 Serine Protein Kinase Bound to ATP

1TQP の概要

• エントリーDOI: 10.2210/pdb1tqp/pdb
• 関連するPDBエントリー: 1TQI 1TQM
• 分子名称: conserved hypothetical protein, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total)
• 機能のキーワード: serine kinase, ribosome
• 由来する生物種: Archaeoglobus fulgidus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33646.20

構造登録者

LaRonde-LeBlanc, N.,Wlodawer, A. (登録日: 2004-06-17, 公開日: 2004-09-28, 最終更新日: 2024-10-30)

主引用文献

LaRonde-LeBlanc, N.,Wlodawer, A.
Crystal Structure of A. fulgidus Rio2 Defines a New Family of Serine Protein Kinases
Structure, 12:1585-1594, 2004

PubMed Abstract: The RIO family of atypical serine/threonine kinases contains two subfamilies, Rio1 and Rio2, highly conserved from archaea to man. Both RIO proteins from Saccharomyces cerevisiae catalyze serine phosphorylation in vitro, and the presence of conserved catalytic residues is required for cell viability. The activity of Rio2 is necessary for rRNA cleavage in 40S ribosomal subunit maturation. We solved the X-ray crystal structure of Archaeoglobus fulgidus Rio2, with and without bound nucleotides, at 2.0 A resolution. The C-terminal RIO domain is indeed structurally homologous to protein kinases, although it differs from known serine kinases in ATP binding and lacks the regions important for substrate binding. Unexpectedly, the N-terminal Rio2-specific domain contains a winged helix fold, seen primarily in DNA-binding proteins. These discoveries have implications in determining the target and function of RIO proteins and define a distinct new family of protein kinases.

PubMed: 15341724
DOI: 10.1016/j.str.2004.06.016

実験手法

X-RAY DIFFRACTION (2.1 Å)