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3lqr

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{{Seed}}
 
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[[Image:3lqr.png|left|200px]]
 
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==Structure of CED-4:CED-3 complex==
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The line below this paragraph, containing "STRUCTURE_3lqr", creates the "Structure Box" on the page.
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<StructureSection load='3lqr' size='340' side='right'caption='[[3lqr]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3lqr]] is a 2 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=3LQR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LQR FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 3.896&#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=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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{{STRUCTURE_3lqr| PDB=3lqr | SCENE= }}
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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=3lqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lqr OCA], [https://pdbe.org/3lqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lqr RCSB], [https://www.ebi.ac.uk/pdbsum/3lqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lqr ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CED4_CAEEL CED4_CAEEL] Isoform a 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. Isoform b prevents PCD.<ref>PMID:1286611</ref> <ref>PMID:8706125</ref> <ref>PMID:9027313</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/lq/3lqr_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=3lqr ConSurf].
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<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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The CED-4 homo-oligomer or apoptosome is required for initiation of programmed cell death in Caenorhabditis elegans by facilitating autocatalytic activation of the CED-3 caspase zymogen. How the CED-4 apoptosome assembles and activates CED-3 remains enigmatic. Here we report the crystal structure of the complete CED-4 apoptosome and show that it consists of eight CED-4 molecules, organized as a tetramer of an asymmetric dimer via a previously unreported interface among AAA(+) ATPases. These eight CED-4 molecules form a funnel-shaped structure. The mature CED-3 protease is monomeric in solution and forms an active holoenzyme with the CED-4 apoptosome, within which the protease activity of CED-3 is markedly stimulated. Unexpectedly, the octameric CED-4 apoptosome appears to bind only two, not eight, molecules of mature CED-3. The structure of the CED-4 apoptosome reveals shared principles for the NB-ARC family of AAA(+) ATPases and suggests a mechanism for the activation of CED-3.
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===Structure of CED-4:CED-3 complex===
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Crystal structure of the Caenorhabditis elegans apoptosome reveals an octameric assembly of CED-4.,Qi S, Pang Y, Hu Q, Liu Q, Li H, Zhou Y, He T, Liang Q, Liu Y, Yuan X, Luo G, Li H, Wang J, Yan N, Shi Y Cell. 2010 Apr 30;141(3):446-57. PMID:20434985<ref>PMID:20434985</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 3lqr" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_20434985}}, adds the Publication Abstract to the page
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*[[Cell death protein 3D structures|Cell death protein 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 20434985 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20434985}}
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__TOC__
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</StructureSection>
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==About this Structure==
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3LQR is a 2 chains structure with 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=3LQR OCA].
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==Reference==
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<ref group="xtra">PMID:20434985</ref><references group="xtra"/>
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[[Category: Caenorhabditis elegans]]
[[Category: Caenorhabditis elegans]]
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[[Category: Pang, Y.]]
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[[Category: Large Structures]]
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[[Category: Qi, S.]]
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[[Category: Pang Y]]
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[[Category: Shi, Y.]]
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[[Category: Qi S]]
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[[Category: Yan, N.]]
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[[Category: Shi Y]]
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[[Category: Alternative splicing]]
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[[Category: Yan N]]
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[[Category: Apoptosis]]
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[[Category: Apoptosome]]
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[[Category: Atp-binding]]
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[[Category: Ced-3]]
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[[Category: Ced-4]]
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[[Category: Mitochondrion]]
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[[Category: Nucleotide-binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 16 08:11:54 2010''
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Current revision

Structure of CED-4:CED-3 complex

PDB ID 3lqr

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