6FH2

Protein arginine kinase McsB in the AMP-PN-bound state

6FH2 の概要

• エントリーDOI: 10.2210/pdb6fh2/pdb
• 関連するPDBエントリー: 6FH1
• 分子名称: Protein-arginine kinase, AMP PHOSPHORAMIDATE, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: protein kinase, protein arginine kinase, protein arginine phosphorylation, phospho-binding domain, signaling protein
• 由来する生物種: Geobacillus stearothermophilus (Bacillus stearothermophilus)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 83309.04

構造登録者

Suskiewicz, M.J.,Heuck, A.,Vu, L.D.,Clausen, T. (登録日: 2018-01-12, 公開日: 2019-02-06, 最終更新日: 2024-01-17)

主引用文献

Suskiewicz, M.J.,Hajdusits, B.,Beveridge, R.,Heuck, A.,Vu, L.D.,Kurzbauer, R.,Hauer, K.,Thoeny, V.,Rumpel, K.,Mechtler, K.,Meinhart, A.,Clausen, T.
Structure of McsB, a protein kinase for regulated arginine phosphorylation.
Nat.Chem.Biol., 15:510-518, 2019

PubMed Abstract: Protein phosphorylation regulates key processes in all organisms. In Gram-positive bacteria, protein arginine phosphorylation plays a central role in protein quality control by regulating transcription factors and marking aberrant proteins for degradation. Here, we report structural, biochemical, and in vivo data of the responsible kinase, McsB, the founding member of an arginine-specific class of protein kinases. McsB differs in structure and mechanism from protein kinases that act on serine, threonine, and tyrosine residues and instead has a catalytic domain related to that of phosphagen kinases (PhKs), metabolic enzymes that phosphorylate small guanidino compounds. In McsB, the PhK-like phosphotransferase domain is structurally adapted to target protein substrates and is accompanied by a novel phosphoarginine (pArg)-binding domain that allosterically controls protein kinase activity. The identification of distinct pArg reader domains in this study points to a remarkably complex signaling system, thus challenging simplistic views of bacterial protein phosphorylation.

PubMed: 30962626
DOI: 10.1038/s41589-019-0265-y

実験手法

X-RAY DIFFRACTION (2.7 Å)