4OTP
Crystal structure of the catalytic domain of the human RioK1 atypical protein kinase in complex with ADP/Mg2+
Summary for 4OTP
| Entry DOI | 10.2210/pdb4otp/pdb |
| Descriptor | Serine/threonine-protein kinase RIO1, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | atypical kinase domain, rio domain, ribosome biogenesis, pre-40s, preribosome, phosphorylation, transferase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 42276.73 |
| Authors | LaRonde, N.A.,Kiburu, I.N. (deposition date: 2014-02-14, release date: 2014-07-02, Last modification date: 2025-03-26) |
| Primary citation | Ferreira-Cerca, S.,Kiburu, I.,Thomson, E.,LaRonde, N.,Hurt, E. Dominant Rio1 kinase/ATPase catalytic mutant induces trapping of late pre-40S biogenesis factors in 80S-like ribosomes. Nucleic Acids Res., 42:8635-8647, 2014 Cited by PubMed Abstract: During eukaryotic ribosome biogenesis, members of the conserved atypical serine/threonine protein kinase family, the RIO kinases (Rio1, Rio2 and Rio3) function in small ribosomal subunit biogenesis. Structural analysis of Rio2 indicated a role as a conformation-sensing ATPase rather than a kinase to regulate its dynamic association with the pre-40S subunit. However, it remained elusive at which step and by which mechanism the other RIO kinase members act. Here, we have determined the crystal structure of the human Rio1-ATP-Mg(2+) complex carrying a phosphoaspartate in the active site indicative of ATPase activity. Structure-based mutations in yeast showed that Rio1's catalytic activity regulates its pre-40S association. Furthermore, we provide evidence that Rio1 associates with a very late pre-40S via its conserved C-terminal domain. Moreover, a rio1 dominant-negative mutant defective in ATP hydrolysis induced trapping of late biogenesis factors in pre-ribosomal particles, which turned out not to be pre-40S but 80S-like ribosomes. Thus, the RIO kinase fold generates a versatile ATPase enzyme, which in the case of Rio1 is activated following the Rio2 step to regulate one of the final 40S maturation events, at which time the 60S subunit is recruited for final quality control check. PubMed: 24948609DOI: 10.1093/nar/gku542 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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