Conformational dynamics of dynamin-like MxA revealed by single-molecule FRET.

ABSTRACT: Human myxovirus resistance protein 1 (MxA) restricts a wide range of viruses and is closely related to the membrane-remodelling GTPase dynamin. The functions of MxA rely on domain rearrangements coupled with GTP hydrolysis cycles. To gain insight into this process, we studied real-time domain dynamics of MxA by single-molecule fluorescence resonance energy transfer. We find that the GTPase domain-bundle-signalling-element (BSE) region can adopt either an 'open' or a 'closed' conformation in all nucleotide-loading conditions. Whereas the open conformation is preferred in nucleotide-free, GDP·AlF₄^--bound and GDP-bound forms, loading of GTP activates the relative movement between the two domains and alters the conformational preference to the 'closed' state. Moreover, fr

SUBMITTER: Chen Y 

PROVIDER: S-EPMC5458555 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature