2rio

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(New page: 200px<br /><applet load="2rio" size="350" color="white" frame="true" align="right" spinBox="true" caption="2rio, resolution 2.40&Aring;" /> '''Structure of the dua...)
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[[Image:2rio.jpg|left|200px]]<br /><applet load="2rio" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2rio, resolution 2.40&Aring;" />
 
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'''Structure of the dual enzyme Ire1 reveals the basis for catalysis and regulation of non-conventional splicing'''<br />
 
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==Overview==
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==Structure of the dual enzyme Ire1 reveals the basis for catalysis and regulation of non-conventional splicing==
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Ire1 is an ancient transmembrane sensor of ER stress with dual protein, kinase and ribonuclease activities. In response to ER stress, Ire1, catalyzes the splicing of target mRNAs in a spliceosome-independent, manner. We have determined the crystal structure of the dual catalytic, region of Ire1at 2.4 A resolution, revealing the fusion of a domain, which, we term the KEN domain, to the protein kinase domain. Dimerization of the, kinase domain composes a large catalytic surface on the KEN domain which, carries out ribonuclease function. We further show that signal induced, trans-autophosphorylation of the kinase domain permits unfettered binding, of nucleotide, which in turn promotes dimerization to compose the, ribonuclease active site. Comparison of Ire1 to a topologically disparate, ribonuclease reveals the convergent evolution of their catalytic, mechanism. These findings provide a basis for understanding the mechanism, of action of RNaseL and other pseudokinases, which represent 10% of the, human kinome.
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<StructureSection load='2rio' size='340' side='right'caption='[[2rio]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2rio]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RIO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RIO FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SR:STRONTIUM+ION'>SR</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2rio FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rio OCA], [https://pdbe.org/2rio PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rio RCSB], [https://www.ebi.ac.uk/pdbsum/2rio PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rio ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/IRE1_YEAST IRE1_YEAST] Senses unfolded proteins in the lumen of the endoplasmic reticulum via its N-terminal domain which leads to enzyme auto-activation. The active endoribonuclease domain splices HAC1 precursor mRNA to produce the mature form which then induces transcription of UPR target genes.<ref>PMID:8663458</ref> <ref>PMID:8670804</ref> <ref>PMID:9323131</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ri/2rio_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2rio ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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2RIO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=SR:'>SR</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Mg Binding Site For Residue A 1102'>AC1</scene>, <scene name='pdbsite=AC2:Sr Binding Site For Residue A 1103'>AC2</scene>, <scene name='pdbsite=AC3:Mg Binding Site For Residue B 2102'>AC3</scene>, <scene name='pdbsite=AC4:Sr Binding Site For Residue B 2103'>AC4</scene>, <scene name='pdbsite=AC5:Adp Binding Site For Residue A 1101'>AC5</scene> and <scene name='pdbsite=AC6:Adp Binding Site For Residue B 2101'>AC6</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RIO OCA].
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*[[Ire1|Ire1]]
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== References ==
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==Reference==
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<references/>
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Structure of the dual enzyme ire1 reveals the basis for catalysis and regulation in nonconventional RNA splicing., Lee KP, Dey M, Neculai D, Cao C, Dever TE, Sicheri F, Cell. 2008 Jan 11;132(1):89-100. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18191223 18191223]
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Cao C]]
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[[Category: Cao, C.]]
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[[Category: Dever TE]]
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[[Category: Dever, T.E.]]
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[[Category: Dey M]]
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[[Category: Dey, M.]]
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[[Category: Lee KP]]
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[[Category: Lee, K.P.]]
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[[Category: Neculai D]]
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[[Category: Neculai, D.]]
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[[Category: Sicheri F]]
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[[Category: Sicheri, F.]]
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[[Category: ADP]]
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[[Category: MG]]
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[[Category: SR]]
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[[Category: atp-binding]]
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[[Category: endoplasmic reticulum]]
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[[Category: glycoprotein]]
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[[Category: hydrolase]]
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[[Category: kinase]]
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[[Category: magnesium]]
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[[Category: membrane]]
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[[Category: metal-binding]]
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[[Category: multifunctional enzyme]]
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[[Category: nucleotide-binding]]
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[[Category: phosphorylation]]
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[[Category: protein-nucleotide complex]]
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[[Category: serine/threonine-protein kinase]]
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[[Category: transcription]]
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[[Category: transcription regulation]]
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[[Category: transferase]]
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[[Category: transmembrane]]
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[[Category: unfolded protein response]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jan 31 11:00:18 2008''
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Current revision

Structure of the dual enzyme Ire1 reveals the basis for catalysis and regulation of non-conventional splicing

PDB ID 2rio

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