2imt

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spinqualitylabelsall models 2imt, resolution 1.49Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

The X-ray Structure of a Bak Homodimer Reveals an Inhibitory Zinc Binding Site

Overview

BAK/BAX-mediated mitochondrial outer-membrane permeabilization (MOMP), drives cell death during development and tissue homeostasis from zebrafish, to humans. In most cancers, this pathway is inhibited by BCL-2 family, antiapoptotic members, which bind and block the action of proapoptotic BCL, proteins. We report the 1.5 A crystal structure of calpain-proteolysed, BAK, cBAK, to reveal a zinc binding site that regulates its activity via, homodimerization. cBAK contains an occluded BH3 peptide binding pocket, that binds a BID BH3 peptide only weakly . Nonetheless, cBAK requires, activation by truncated BID to induce cytochrome c release in mitochondria, isolated from bak/bax double-knockout mouse embryonic fibroblasts. The, BAK-mediated MOMP is inhibited by low micromolar zinc levels. This, inhibition is alleviated by mutation of the zinc-coordination site in BAK., Our results link directly the antiapoptotic effects of zinc to BAK.

About this Structure

2IMT is a Single protein structure of sequence from Homo sapiens with ZN as ligand. Full crystallographic information is available from OCA.

Reference

The X-ray structure of a BAK homodimer reveals an inhibitory zinc binding site., Moldoveanu T, Liu Q, Tocilj A, Watson M, Shore G, Gehring K, Mol Cell. 2006 Dec 8;24(5):677-88. PMID:17157251

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