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1ty4

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[[Image:1ty4.gif|left|200px]]<br /><applet load="1ty4" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ty4, resolution 2.2&Aring;" />
 
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'''Crystal structure of a CED-9/EGL-1 complex'''<br />
 
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==Overview==
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==Crystal structure of a CED-9/EGL-1 complex==
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Programmed cell death in Caenorhabditis elegans is initiated by the binding of EGL-1 to CED-9, which disrupts the CED-4/CED-9 complex and allows CED-4 to activate the cell-killing caspase CED-3. Here we demonstrate that the C-terminal half of EGL-1 is necessary and sufficient for binding to CED-9 and for killing cells. Structure of the EGL-1/CED-9 complex revealed that EGL-1 adopts an extended alpha-helical conformation and induces substantial structural rearrangements in CED-9 upon binding. EGL-1 interface mutants failed to bind to CED-9 or to release CED-4 from the CED-4/CED-9 complex, and were unable to induce cell death in vivo. A surface patch on CED-9, different from that required for binding to EGL-1, was identified to be responsible for binding to CED-4. These data suggest a working mechanism for the release of CED-4 from the CED-4/CED-9 complex upon EGL-1 binding and provide a mechanistic framework for understanding apoptosis activation in C. elegans.
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<StructureSection load='1ty4' size='340' side='right'caption='[[1ty4]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ty4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TY4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TY4 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]] 2.2&#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=MSE:SELENOMETHIONINE'>MSE</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=1ty4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ty4 OCA], [https://pdbe.org/1ty4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ty4 RCSB], [https://www.ebi.ac.uk/pdbsum/1ty4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ty4 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CED9_CAEEL CED9_CAEEL] Plays a major role in programmed cell death (PCD, apoptosis). Egl-1 binds to and directly inhibits the activity of ced-9, releasing the cell death activator ced-4 from a ced-9/ced-4 containing protein complex and allowing ced-4 to activate the cell-killing caspase ced-3.<ref>PMID:7907274</ref> <ref>PMID:9024666</ref> <ref>PMID:9027313</ref> <ref>PMID:9604928</ref> <ref>PMID:10688797</ref> <ref>PMID:15383288</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/ty/1ty4_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=1ty4 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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1TY4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TY4 OCA].
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*[[Cell death protein 3D structures|Cell death protein 3D structures]]
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== References ==
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==Reference==
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<references/>
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Structural, biochemical, and functional analyses of CED-9 recognition by the proapoptotic proteins EGL-1 and CED-4., Yan N, Gu L, Kokel D, Chai J, Li W, Han A, Chen L, Xue D, Shi Y, Mol Cell. 2004 Sep 24;15(6):999-1006. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15383288 15383288]
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__TOC__
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</StructureSection>
[[Category: Caenorhabditis elegans]]
[[Category: Caenorhabditis elegans]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Gu, L.]]
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[[Category: Gu L]]
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[[Category: Kokel, D.]]
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[[Category: Kokel D]]
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[[Category: Shi, Y.]]
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[[Category: Shi Y]]
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[[Category: Xue, D.]]
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[[Category: Xue D]]
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[[Category: Yan, N.]]
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[[Category: Yan N]]
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[[Category: apoptosis]]
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[[Category: bcl-2 family proteins]]
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[[Category: ced-9]]
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[[Category: egl-1]]
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[[Category: recognition]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:18:32 2008''
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Current revision

Crystal structure of a CED-9/EGL-1 complex

PDB ID 1ty4

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