7K02
The crystal structure of a BAK dimer activated by detergent
Summary for 7K02
| Entry DOI | 10.2210/pdb7k02/pdb |
| Related | 4U2V |
| Descriptor | Bcl-2 homologous antagonist/killer (1 entity in total) |
| Functional Keywords | bak, bh3-in-groove dimer, bcl-2 fold, pore forming, proapoptotic, apoptosis |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 6 |
| Total formula weight | 81602.37 |
| Authors | Birkinshaw, R.W.,Czabotar, P.E. (deposition date: 2020-09-02, release date: 2021-03-31, Last modification date: 2023-10-18) |
| Primary citation | Birkinshaw, R.W.,Iyer, S.,Lio, D.,Luo, C.S.,Brouwer, J.M.,Miller, M.S.,Robin, A.Y.,Uren, R.T.,Dewson, G.,Kluck, R.M.,Colman, P.M.,Czabotar, P.E. Structure of detergent-activated BAK dimers derived from the inert monomer. Mol.Cell, 81:2123-, 2021 Cited by PubMed Abstract: A body of data supports the existence of core (α2-α5) dimers of BAK and BAX in the oligomeric, membrane-perturbing conformation of these essential apoptotic effector molecules. Molecular structures for these dimers have only been captured for truncated constructs encompassing the core domain alone. Here, we report a crystal structure of BAK α2-α8 dimers (i.e., minus its flexible N-terminal helix and membrane-anchoring C-terminal segment) that has been obtained through the activation of monomeric BAK with the detergent C12E8. Core dimers are evident, linked through the crystal by contacts via latch (α6-α8) domains. This crystal structure shows activated BAK dimers with the extended latch domain present. Our data provide direct evidence for the conformational change converting BAK from inert monomer to the functional dimer that destroys mitochondrial integrity. This dimer is the smallest functional unit for recombinant BAK or BAX described so far. PubMed: 33794146DOI: 10.1016/j.molcel.2021.03.014 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.4 Å) |
Structure validation
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