3SFZ: Crystal Structure Of Full-Length Murine Apaf-1

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.
PDB ID: 3SFZDownload
MMDB ID: 92950
PDB Deposition Date: 2011/6/14
Updated in MMDB: 2011/08
Experimental Method:
x-ray diffraction
Resolution: 3  Å
Source Organism:
Similar Structures:
Biological Unit for 3SFZ: monomeric; determined by author and by software (PISA)
Molecular Components in 3SFZ
Label Count Molecule
Protein (1 molecule)
Apoptotic Peptidase Activating Factor 1
Molecule annotation
Chemicals (6 molecules)
* Click molecule labels to explore molecular sequence information.

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