2rio

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[[Image:2rio.jpg|left|200px]]
 
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{{Structure
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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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|PDB= 2rio |SIZE=350|CAPTION= <scene name='initialview01'>2rio</scene>, resolution 2.40&Aring;
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<StructureSection load='2rio' size='340' side='right'caption='[[2rio]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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|SITE= <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>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SR:STRONTIUM+ION'>SR</scene>
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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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|ACTIVITY=
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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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|GENE= IRE1, ERN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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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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|DOMAIN=
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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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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2rio FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rio OCA], [http://www.ebi.ac.uk/pdbsum/2rio PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2rio RCSB]</span>
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== Function ==
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}}
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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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'''Structure of the dual enzyme Ire1 reveals the basis for catalysis and regulation of non-conventional splicing'''
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==See Also==
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*[[Ire1|Ire1]]
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== References ==
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==Overview==
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<references/>
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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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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2RIO is a [[Single protein]] structure of sequence from [http://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].
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/18191223 18191223]
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[[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: 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 Mon Mar 31 05:00:51 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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