6FDO

Rio2 structure

Summary for 6FDO

• Entry DOI: 10.2210/pdb6fdo/pdb
• Descriptor: Serine/threonine-protein kinase RIO2 (2 entities in total)
• Functional Keywords: kinase, hydrolase
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 81464.49

Authors

Fribourg, S. (deposition date: 2017-12-26, release date: 2019-01-30, Last modification date: 2024-05-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.6 Å)