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| | <StructureSection load='1tqm' size='340' side='right'caption='[[1tqm]], [[Resolution|resolution]] 1.99Å' scene=''> | | <StructureSection load='1tqm' size='340' side='right'caption='[[1tqm]], [[Resolution|resolution]] 1.99Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1tqm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arcfu Arcfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TQM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1TQM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1tqm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus_DSM_4304 Archaeoglobus fulgidus DSM 4304]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TQM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TQM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene></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]] 1.99Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1tqi|1tqi]], [[1tqp|1tqp]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RIO2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224325 ARCFU])</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=1tqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tqm OCA], [https://pdbe.org/1tqm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tqm RCSB], [https://www.ebi.ac.uk/pdbsum/1tqm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tqm ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1tqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tqm OCA], [http://pdbe.org/1tqm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tqm RCSB], [http://www.ebi.ac.uk/pdbsum/1tqm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tqm ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/RIO2_ARCFU RIO2_ARCFU] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arcfu]] | + | [[Category: Archaeoglobus fulgidus DSM 4304]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: LaRonde-LeBlanc, N]] | + | [[Category: LaRonde-LeBlanc N]] |
| - | [[Category: Wlodawer, A]] | + | [[Category: Wlodawer A]] |
| - | [[Category: Amppnp]]
| + | |
| - | [[Category: Anp]]
| + | |
| - | [[Category: Ribosome]]
| + | |
| - | [[Category: Serine kinase]]
| + | |
| Structural highlights
Function
RIO2_ARCFU
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The RIO family of atypical serine/threonine kinases contains two subfamilies, Rio1 and Rio2, highly conserved from archaea to man. Both RIO proteins from Saccharomyces cerevisiae catalyze serine phosphorylation in vitro, and the presence of conserved catalytic residues is required for cell viability. The activity of Rio2 is necessary for rRNA cleavage in 40S ribosomal subunit maturation. We solved the X-ray crystal structure of Archaeoglobus fulgidus Rio2, with and without bound nucleotides, at 2.0 A resolution. The C-terminal RIO domain is indeed structurally homologous to protein kinases, although it differs from known serine kinases in ATP binding and lacks the regions important for substrate binding. Unexpectedly, the N-terminal Rio2-specific domain contains a winged helix fold, seen primarily in DNA-binding proteins. These discoveries have implications in determining the target and function of RIO proteins and define a distinct new family of protein kinases.
Crystal structure of A. fulgidus Rio2 defines a new family of serine protein kinases.,LaRonde-LeBlanc N, Wlodawer A Structure. 2004 Sep;12(9):1585-94. PMID:15341724[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ LaRonde-LeBlanc N, Wlodawer A. Crystal structure of A. fulgidus Rio2 defines a new family of serine protein kinases. Structure. 2004 Sep;12(9):1585-94. PMID:15341724 doi:10.1016/j.str.2004.06.016
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