1TY4: Crystal Structure Of A Ced-9EGL-1 Complex

Programmed cell death in Caenorhabditis elegans is initiated by the binding of EGL-1 to CED-9, which disrupts the CED-4/CED-9 complex and allows CED-4 to activate the cell-killing caspase CED-3. Here we demonstrate that the C-terminal half of EGL-1 is necessary and sufficient for binding to CED-9 and for killing cells. Structure of the EGL-1/CED-9 complex revealed that EGL-1 adopts an extended alpha-helical conformation and induces substantial structural rearrangements in CED-9 upon binding. EGL-1 interface mutants failed to bind to CED-9 or to release CED-4 from the CED-4/CED-9 complex, and were unable to induce cell death in vivo. A surface patch on CED-9, different from that required for binding to EGL-1, was identified to be responsible for binding to CED-4. These data suggest a working mechanism for the release of CED-4 from the CED-4/CED-9 complex upon EGL-1 binding and provide a mechanistic framework for understanding apoptosis activation in C. elegans.
PDB ID: 1TY4Download
MMDB ID: 29494
PDB Deposition Date: 2004/7/7
Updated in MMDB: 2004/12
Experimental Method:
x-ray diffraction
Resolution: 2.2  Å
Source Organism:
Similar Structures:
Biological Unit for 1TY4: tetrameric; determined by author
Molecular Components in 1TY4
Label Count Molecule
Proteins (4 molecules)
Apoptosis Regulator Ced-9(Gene symbol: ced-9)
Molecule annotation
EGG Laying Defective Egl-1, Programmed Cell Death Activator(Gene symbol: egl-1)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB