3SFZ

Crystal structure of full-length murine Apaf-1


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.298 
  • R-Value Work: 0.235 
  • R-Value Observed: 0.235 

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Literature

Crystal structure of full-length Apaf-1: how the death signal is relayed in the mitochondrial pathway of apoptosis.

Reubold, T.F.Wohlgemuth, S.Eschenburg, S.

(2011) Structure 19: 1074-1083

  • DOI: https://doi.org/10.1016/j.str.2011.05.013
  • Primary Citation of Related Structures:  
    3SFZ, 3SHF

  • PubMed Abstract: 

    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 Å 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 Å resolution and we show that proper function of Apaf-1 relies on R265 in the vicinity of the bound nucleotide.


  • Organizational Affiliation

    Insitute for Biophysical Chemistry, Hannover Medical School, OE 4350, D-30625, Hannover, Germany.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Apoptotic peptidase activating factor 11,249Mus musculusMutation(s): 0 
Gene Names: Apaf1
UniProt
Find proteins for O88879 (Mus musculus)
Explore O88879 
Go to UniProtKB:  O88879
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO88879
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.298 
  • R-Value Work: 0.235 
  • R-Value Observed: 0.235 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 72.65α = 90
b = 113.07β = 90
c = 243.56γ = 90
Software Package:
Software NamePurpose
XSCALEdata scaling
CNSrefinement
PDB_EXTRACTdata extraction
ADSCdata collection
XDSdata reduction
PHASERphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2011-08-24
    Type: Initial release