4gyg

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4gyg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gyg OCA], [https://pdbe.org/4gyg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gyg RCSB], [https://www.ebi.ac.uk/pdbsum/4gyg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gyg ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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.

ATPase-dependent role of the atypical kinase Rio2 on the evolving pre-40S ribosomal subunit.,Ferreira-Cerca S, Sagar V, Schafer T, Diop M, Wesseling AM, Lu H, Chai E, Hurt E, Laronde-Leblanc N Nat Struct Mol Biol. 2012 Dec;19(12):1316-23. doi: 10.1038/nsmb.2403. Epub 2012, Oct 28. PMID:23104056<ref>PMID:23104056</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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