3sfz | pdb_00003sfz

Crystal structure of full-length murine Apaf-1

spinqualitylabelsall models 3sfz, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3sfz is a 1 chain structure with sequence from Lk3 transgenic mice. The September 2014 RCSB PDB Molecule of the Month feature on Apoptosomes by David Goodsell is 10.2210/rcsb_pdb/mom_2014_9. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, GBL Related: 3shf Gene: Apaf1 (LK3 transgenic mice) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [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). 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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