Native ESI-MS and Collision Induced Unfolding (CIU) of the Complex between Bacterial Elongation Factor-Tu and the Antibiotic Enacyloxin IIa

Abstract

Raw native-MS and IM-MS data supporting publication in JASMS.

Abstract:

Collision induced unfolding (CIU) of protein ions, monitored by ion mobility-mass spectrometry (IM-MS), can be used to assess the stability of their compact gas-phase fold, and hence provide structural information. The bacterial elongation factor EF-Tu, a key protein for protein translation in prokaryotes, and hence a promising antibiotic target, has been studied by CIU. The major [M+12H]12+ ion of EF-Tu unfolded in collision with Ar atoms between 40 and 50 V, corresponding to an Elab energy of 480-500 eV. Binding of the cofactor analogue GDPNP and the antibiotic enacyloxin IIa stabilized the compact fold of EF-Tu, although dissociation of the latter from the complex diminished its stabilizing effect at higher collision energies