2rio

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Current revision (09:22, 21 February 2024) (edit) (undo)
 
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<StructureSection load='2rio' size='340' side='right'caption='[[2rio]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='2rio' size='340' side='right'caption='[[2rio]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== 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/Atcc_18824 Atcc 18824]. 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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<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='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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</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IRE1, ERN1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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>
<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>
<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>
</table>
</table>
== Function ==
== 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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[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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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].
</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].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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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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:18191223<ref>PMID:18191223</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 2rio" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 18824]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Cao, C]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Dever, T E]]
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[[Category: Cao C]]
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[[Category: Dey, M]]
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[[Category: Dever TE]]
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[[Category: Lee, K P]]
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[[Category: Dey M]]
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[[Category: Neculai, D]]
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[[Category: Lee KP]]
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[[Category: Sicheri, F]]
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[[Category: Neculai D]]
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[[Category: Atp-binding]]
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[[Category: Sicheri F]]
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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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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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Proteopedia Page Contributors and Editors (what is this?)

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