A new perspective on membrane-embedded Bax oligomers using DEER and bioresistant orthogonal spin labels.

ABSTRACT: Bax is a Bcl-2 protein crucial for apoptosis initiation and execution, whose active conformation is only partially understood. Dipolar EPR spectroscopy has proven to be a valuable tool to determine coarse-grained models of membrane-embedded Bcl-2 proteins. Here we show how the combination of spectroscopically distinguishable nitroxide and gadolinium spin labels and Double Electron-Electron Resonance can help to gain new insights into the quaternary structure of active, membrane-embedded Bax oligomers. We show that attaching labels bulkier than the conventional MTSL may affect Bax fold and activity, depending on the protein/label combination. However, we identified a suitable pair of spectroscopically distinguishable labels, which allows to study complex distance networks in the oligomers t

SUBMITTER: Teucher M 

PROVIDER: S-EPMC6737250 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature