Single-molecule studies of conformational states and dynamics in the ABC importer OpuA

  • Konstantinos Tassis
  • , Ruslan Vietrov
  • , Matthijs de Koning
  • , Marijn de Boer
  • , Giorgos Gouridis*
  • , Thorben Cordes*
  • *Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

9 Citations (Scopus)
79 Downloads (Pure)

Abstract

The current model of active transport via ABC importers is mostly based on structural, biochemical and genetic data. We here establish single-molecule Förster resonance energy transfer (smFRET) assays to monitor the conformational states and heterogeneity of the osmoregulatory type I ABC importer OpuA from Lactococcus lactis. We present data probing both intradomain distances that elucidate conformational changes within the substrate-binding domain (SBD) OpuAC, and interdomain distances between SBDs or transmembrane domains. Using this methodology, we studied ligand-binding mechanisms, as well as ATP and glycine betaine dependences of conformational changes. Our work expands the scope of smFRET investigations towards a class of so far unstudied ABC importers, and paves the way for a full understanding of their transport cycle in the future.

Original languageEnglish
Pages (from-to)717-734
Number of pages18
JournalFEBS Letters
Volume595
Issue number6
DOIs
Publication statusPublished - Mar-2021

Keywords

  • ABC transporter
  • conformational dynamics
  • membrane transport
  • osmoregulation
  • single-molecule Foerster resonance energy transfer
  • substrate-binding domains

Fingerprint

Dive into the research topics of 'Single-molecule studies of conformational states and dynamics in the ABC importer OpuA'. Together they form a unique fingerprint.

Cite this