6FDM

Human Rio2 kinase structure

6FDM の概要

• エントリーDOI: 10.2210/pdb6fdm/pdb
• 分子名称: Serine/threonine-protein kinase RIO2, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: kinase, ribosome, transferase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 146453.04

構造登録者

Fribourg, S. (登録日: 2017-12-26, 公開日: 2019-01-30, 最終更新日: 2024-05-08)

主引用文献

Maurice, F.,Perebaskine, N.,Thore, S.,Fribourg, S.
In vitro dimerization of human RIO2 kinase.
Rna Biol., 16:1633-1642, 2019

PubMed Abstract: RIO proteins form a conserved family of atypical protein kinases. RIO2 is a serine/threonine protein kinase/ATPase involved in pre-40S ribosomal maturation. Current crystal structures of archaeal and fungal Rio2 proteins report a monomeric form of the protein. Here, we describe three atomic structures of the human RIO2 kinase showing that it forms a homodimer . Upon self-association, each protomer ATP-binding pocket is partially remodelled and found in an apostate. The homodimerization is mediated by key residues previously shown to be responsible for ATP binding and catalysis. This unusual protein kinase dimer reveals an intricate mechanism where identical residues are involved in substrate binding and oligomeric state formation. We speculate that such an oligomeric state might be formed also and might function in maintaining the protein in an inactive state and could be employed during import.

PubMed: 31390939
DOI: 10.1080/15476286.2019.1653679

実験手法

X-RAY DIFFRACTION (2.1 Å)