Probing Polytopic Membrane Protein-Substrate Interactions by Luminescence Resonance Energy Transfer.

ABSTRACT: Integral membrane proteins play essential roles in all living systems; however, major technical hurdles challenge analyses of this class of proteins. Biophysical approaches that provide structural information to complement and leverage experimentally determined and computationally predicted structures are urgently needed. Herein we present the application of luminescence resonance energy transfer (LRET) for investigating the interactions of the polytopic membrane-bound oligosaccharyl transferases (OTases) with partner substrates. Monomeric OTases, such as the PglBs from Campylobacter jejuni and Campylobacter lari, catalyze transfer of glycans from membrane-associated undecaprenol diphosphate-linked substrates to proteins in the bacterial periplasm. LRET-based distance measurements are enab

SUBMITTER: Musial-Siwek M 

PROVIDER: S-EPMC5480290 | biostudies-literature | 2016 Mar

REPOSITORIES: biostudies-literature