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3shf

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Crystal structure of the R265S mutant of full-length murine Apaf-1

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Retrieved from "http://52.214.119.220/wiki/index.php/3shf"

Categories: Large Structures | Mus musculus | Eschenburg S | Reubold TF

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 <StructureSection load='3shf' size='340' side='right'caption='[[3shf]], [[Resolution|resolution]] 3.55&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3shf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SHF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SHF FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3shf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SHF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SHF FirstGlance]. <br>
-</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=GBL:GAMMA-BUTYROLACTONE'>GBL</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.55&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3sfz|3sfz]]</div></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=GBL:GAMMA-BUTYROLACTONE'>GBL</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Apaf1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3shf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3shf OCA], [https://pdbe.org/3shf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3shf RCSB], [https://www.ebi.ac.uk/pdbsum/3shf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3shf ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/APAF_MOUSE APAF_MOUSE]] Oligomeric Apaf-1 mediates the cytochrome c-dependent autocatalytic activation of pro-caspase-9 (Apaf-3), leading to the activation of caspase-3 and apoptosis. This activation requires ATP (By similarity).
+[https://www.uniprot.org/uniprot/APAF_MOUSE APAF_MOUSE] Oligomeric Apaf-1 mediates the cytochrome c-dependent autocatalytic activation of pro-caspase-9 (Apaf-3), leading to the activation of caspase-3 and apoptosis. This activation requires ATP (By similarity).
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The apoptotic protease-activating factor 1 (Apaf-1) relays the death signal in the mitochondrial pathway of apoptosis. Apaf-1 oligomerizes on binding of mitochondrially released cytochrome c into the heptameric apoptosome complex to ignite the downstream cascade of caspases. Here, we present the 3.0 A crystal structure of full-length murine Apaf-1 in the absence of cytochrome c. The structure shows how the mammalian death switch is kept in its "off" position. By comparing the off state with a recent cryo-electron microscopy derived model of Apaf-1 in its apoptosomal conformation, we depict the molecular events that transform Apaf-1 from autoinhibited monomer to a building block of the caspase-activating apoptosome. Moreover, we have solved the crystal structure of the R265S mutant of full-length murine Apaf-1 in the absence of cytochrome c to 3.55 A resolution and we show that proper function of Apaf-1 relies on R265 in the vicinity of the bound nucleotide.
-Crystal structure of full-length apaf-1: how the death signal is relayed in the mitochondrial pathway of apoptosis.,Reubold TF, Wohlgemuth S, Eschenburg S Structure. 2011 Aug 10;19(8):1074-83. PMID:21827944<ref>PMID:21827944</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3shf" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Apoptotic protease-activating factor-1 3D structures|Apoptotic protease-activating factor-1 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Lk3 transgenic mice]]
+[[Category: Mus musculus]]
-[[Category: Eschenburg, S]]
+[[Category: Eschenburg S]]
-[[Category: Reubold, T F]]
+[[Category: Reubold TF]]
-[[Category: Adenine nucleotide]]
-[[Category: Apoptosis]]
-[[Category: Cytochrome c]]
-[[Category: Cytosol]]
-[[Category: Procaspase-9]]
-[[Category: Tandem beta-propeller]]

3shf

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Crystal structure of the R265S mutant of full-length murine Apaf-1

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