3shf: Difference between revisions
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<StructureSection load='3shf' size='340' side='right'caption='[[3shf]], [[Resolution|resolution]] 3.55Å' scene=''> | <StructureSection load='3shf' size='340' side='right'caption='[[3shf]], [[Resolution|resolution]] 3.55Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3shf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <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=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.55Å</td></tr> | ||
<tr id=' | <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='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> | <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> | </table> | ||
== Function == | == 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). | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: Eschenburg | [[Category: Eschenburg S]] | ||
[[Category: Reubold | [[Category: Reubold TF]] | ||
Latest revision as of 13:26, 6 November 2024
Crystal structure of the R265S mutant of full-length murine Apaf-1Crystal structure of the R265S mutant of full-length murine Apaf-1
Structural highlights
FunctionAPAF_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). Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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