4GYI

Crystal structure of the Rio2 kinase-ADP/Mg2+-phosphoaspartate complex from Chaetomium thermophilum

Summary for 4GYI

• Entry DOI: 10.2210/pdb4gyi/pdb
• Related: 4GYG
• Descriptor: Rio2 kinase, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: protein kinase, adp complex, phosphoaspartate, acyl-phosphate, ribosome biogenesis, ser/thr protein kinase, ribosome biogenesis; ribosomal rna processing; pre-40s maturation, pre-40s, phosphorylation, transferase
• Biological source: Chaetomium thermophilum
• Total number of polymer chains: 1
• Total formula weight: 45347.47

Authors

Ferreira-Cerca, S.,Sagar, V.,Schafer, T.,Diop, M.,Wesseling, A.M.,Lu, H.,Chai, E.,Hurt, E.,LaRonde-LeBlanc, N. (deposition date: 2012-09-05, release date: 2012-10-17, Last modification date: 2023-09-13)

Primary citation

Ferreira-Cerca, S.,Sagar, V.,Schafer, T.,Diop, M.,Wesseling, A.M.,Lu, H.,Chai, E.,Hurt, E.,Laronde-Leblanc, N.
ATPase-dependent role of the atypical kinase Rio2 on the evolving pre-40S ribosomal subunit.
Nat.Struct.Mol.Biol., 19:1316-1323, 2012

PubMed Abstract: Ribosome synthesis involves dynamic association of ribosome-biogenesis factors with evolving preribosomal particles. Rio2 is an atypical protein kinase required for pre-40S subunit maturation. We report the crystal structure of eukaryotic Rio2-ATP-Mg(2+) complex. The active site contains ADP-Mg(2+) and a phosphoaspartate intermediate typically found in Na(+), K(+) and Ca(2+) ATPases but not protein kinases. Consistent with this finding, ctRio2 exhibits a robust ATPase activity in vitro. In vivo, Rio2 docks on the ribosome, with its active site occluded and its flexible loop positioned to interact with the pre-40S subunit. Moreover, Rio2 catalytic activity is required for its dissociation from the ribosome, a necessary step in pre-40S maturation. We propose that phosphoryl transfer from ATP to Asp257 in Rio2's active site and subsequent hydrolysis of the aspartylphosphate could be a trigger to power late cytoplasmic 40S subunit biogenesis.

PubMed: 23104056
DOI: 10.1038/nsmb.2403

Experimental method

X-RAY DIFFRACTION (2.2 Å)