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| | <StructureSection load='6fdo' size='340' side='right'caption='[[6fdo]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='6fdo' size='340' side='right'caption='[[6fdo]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6fdo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FDO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FDO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6fdo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FDO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FDO FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RIOK2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></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=6fdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fdo OCA], [https://pdbe.org/6fdo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fdo RCSB], [https://www.ebi.ac.uk/pdbsum/6fdo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fdo ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6fdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fdo OCA], [http://pdbe.org/6fdo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fdo RCSB], [http://www.ebi.ac.uk/pdbsum/6fdo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fdo ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RIOK2_HUMAN RIOK2_HUMAN]] Serine/threonine-protein kinase involved in the final steps of cytoplasmic maturation of the 40S ribosomal subunit. Involved in export of the 40S pre-ribosome particles (pre-40S) from the nucleus to the cytoplasm. Its kinase activity is required for the release of NOB1, PNO1 and LTV1 from the late pre-40S and the processing of 18S-E pre-rRNA to the mature 18S rRNA (PubMed:19564402). Regulates the timing of the metaphase-anaphase transition during mitotic progression, and its phosphorylation, most likely by PLK1, regulates this function (PubMed:21880710).<ref>PMID:16037817</ref> <ref>PMID:19564402</ref> <ref>PMID:21880710</ref> | + | [https://www.uniprot.org/uniprot/RIOK2_HUMAN RIOK2_HUMAN] Serine/threonine-protein kinase involved in the final steps of cytoplasmic maturation of the 40S ribosomal subunit. Involved in export of the 40S pre-ribosome particles (pre-40S) from the nucleus to the cytoplasm. Its kinase activity is required for the release of NOB1, PNO1 and LTV1 from the late pre-40S and the processing of 18S-E pre-rRNA to the mature 18S rRNA (PubMed:19564402). Regulates the timing of the metaphase-anaphase transition during mitotic progression, and its phosphorylation, most likely by PLK1, regulates this function (PubMed:21880710).<ref>PMID:16037817</ref> <ref>PMID:19564402</ref> <ref>PMID:21880710</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6fdo" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6fdo" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Non-specific serine/threonine protein kinase]]
| + | [[Category: Fribourg S]] |
| - | [[Category: Fribourg, S]] | + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Kinase]]
| + | |
| Structural highlights
Function
RIOK2_HUMAN Serine/threonine-protein kinase involved in the final steps of cytoplasmic maturation of the 40S ribosomal subunit. Involved in export of the 40S pre-ribosome particles (pre-40S) from the nucleus to the cytoplasm. Its kinase activity is required for the release of NOB1, PNO1 and LTV1 from the late pre-40S and the processing of 18S-E pre-rRNA to the mature 18S rRNA (PubMed:19564402). Regulates the timing of the metaphase-anaphase transition during mitotic progression, and its phosphorylation, most likely by PLK1, regulates this function (PubMed:21880710).[1] [2] [3]
Publication Abstract from PubMed
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 in vitro. 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 in vitro 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 in vivo and might function in maintaining the protein in an inactive state and could be employed during import.
In vitro dimerization of human RIO2 kinase.,Maurice F, Perebaskine N, Thore S, Fribourg S RNA Biol. 2019 Nov;16(11):1633-1642. doi: 10.1080/15476286.2019.1653679. Epub, 2019 Aug 14. PMID:31390939[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Rouquette J, Choesmel V, Gleizes PE. Nuclear export and cytoplasmic processing of precursors to the 40S ribosomal subunits in mammalian cells. EMBO J. 2005 Aug 17;24(16):2862-72. doi: 10.1038/sj.emboj.7600752. Epub 2005 Jul , 28. PMID:16037817 doi:http://dx.doi.org/10.1038/sj.emboj.7600752
- ↑ Zemp I, Wild T, O'Donohue MF, Wandrey F, Widmann B, Gleizes PE, Kutay U. Distinct cytoplasmic maturation steps of 40S ribosomal subunit precursors require hRio2. J Cell Biol. 2009 Jun 29;185(7):1167-80. PMID:19564402 doi:http://dx.doi.org/jcb.200904048
- ↑ Liu T, Deng M, Li J, Tong X, Wei Q, Ye X. Phosphorylation of right open reading frame 2 (Rio2) protein kinase by polo-like kinase 1 regulates mitotic progression. J Biol Chem. 2011 Oct 21;286(42):36352-60. doi: 10.1074/jbc.M111.250175. Epub, 2011 Aug 31. PMID:21880710 doi:http://dx.doi.org/10.1074/jbc.M111.250175
- ↑ Maurice F, Perebaskine N, Thore S, Fribourg S. In vitro dimerization of human RIO2 kinase. RNA Biol. 2019 Nov;16(11):1633-1642. doi: 10.1080/15476286.2019.1653679. Epub, 2019 Aug 14. PMID:31390939 doi:http://dx.doi.org/10.1080/15476286.2019.1653679
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