2rio

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[[Image:2rio.jpg|left|200px]]
[[Image:2rio.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 2rio |SIZE=350|CAPTION= <scene name='initialview01'>2rio</scene>, resolution 2.40&Aring;
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The line below this paragraph, containing "STRUCTURE_2rio", creates the "Structure Box" on the page.
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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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|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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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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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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|DOMAIN=
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{{STRUCTURE_2rio| PDB=2rio | SCENE= }}
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|RELATEDENTRY=
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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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'''Structure of the dual enzyme Ire1 reveals the basis for catalysis and regulation of non-conventional splicing'''
'''Structure of the dual enzyme Ire1 reveals the basis for catalysis and regulation of non-conventional splicing'''
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[[Category: Neculai, D.]]
[[Category: Neculai, D.]]
[[Category: Sicheri, F.]]
[[Category: Sicheri, F.]]
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[[Category: atp-binding]]
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[[Category: Atp-binding]]
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[[Category: endoplasmic reticulum]]
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[[Category: Endoplasmic reticulum]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: serine/threonine-protein kinase]]
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[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 16:58:41 2008''
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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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Revision as of 13:58, 4 May 2008

Image:2rio.jpg

Template:STRUCTURE 2rio

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


Overview

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.

About this Structure

2RIO is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sun May 4 16:58:41 2008

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OCA

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