1TY4

Crystal structure of a CED-9/EGL-1 complex

Summary for 1TY4

• Entry DOI: 10.2210/pdb1ty4/pdb
• Descriptor: Apoptosis regulator ced-9, EGg Laying defective EGL-1, programmed cell death activator (3 entities in total)
• Functional Keywords: apoptosis, ced-9, egl-1, bcl-2 family proteins, recognition
• Biological source: Caenorhabditis elegans; More
• Cellular location: Endomembrane system; Peripheral membrane protein: P41958
• Total number of polymer chains: 4
• Total formula weight: 53532.40

Authors

Yan, N.,Gu, L.,Kokel, D.,Xue, D.,Shi, Y. (deposition date: 2004-07-07, release date: 2004-09-28, Last modification date: 2024-11-20)

Primary citation

Yan, N.,Gu, L.,Kokel, D.,Chai, J.,Li, W.,Han, A.,Chen, L.,Xue, D.,Shi, Y.
Structural, Biochemical, and Functional Analyses of CED-9 Recognition by the Proapoptotic Proteins EGL-1 and CED-4
Mol.Cell, 15:999-1006, 2004

PubMed Abstract: 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.

PubMed: 15383288
DOI: 10.1016/j.molcel.2004.08.022

Experimental method

X-RAY DIFFRACTION (2.2 Å)