4BD6: Bax Domain Swapped Dimer In Complex With Baxbh3

In stressed cells, apoptosis ensues when Bcl-2 family members Bax or Bak oligomerize and permeabilize the mitochondrial outer membrane. Certain BH3-only relatives can directly activate them to mediate this pivotal, poorly understood step. To clarify the conformational changes that induce Bax oligomerization, we determined crystal structures of BaxDeltaC21 treated with detergents and BH3 peptides. The peptides bound the Bax canonical surface groove but, unlike their complexes with prosurvival relatives, dissociated Bax into two domains. The structures define the sequence signature of activator BH3 domains and reveal how they can activate Bax via its groove by favoring release of its BH3 domain. Furthermore, Bax helices alpha2-alpha5 alone adopted a symmetric homodimer structure, supporting the proposal that two Bax molecules insert their BH3 domain into each other's surface groove to nucleate oligomerization. A planar lipophilic surface on this homodimer may engage the membrane. Our results thus define critical Bax transitions toward apoptosis.
PDB ID: 4BD6Download
MMDB ID: 107533
PDB Deposition Date: 2012/10/5
Updated in MMDB: 2013/02
Experimental Method:
x-ray diffraction
Resolution: 2.49  Å
Source Organism:
Similar Structures:
Biological Unit for 4BD6: tetrameric; determined by author and by software (PISA)
Molecular Components in 4BD6
Label Count Molecule
Proteins (4 molecules)
Apoptosis Regulator BAX(Gene symbol: BAX)
Molecule annotation
Apoptosis Regulator BAX(Gene symbol: BAX)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB