Catalytic activity of MsbA reconstituted in nanodisc particles is modulated by remote interactions with the bilayer

Takeaki Kawai, Jose M.M. Caaveiro, Ryota Abe, Toyomasa Katagiri, Kouhei Tsumoto

Research output: Contribution to journalArticlepeer-review

39 Citations (Scopus)

Abstract

ATP-binding cassette (ABC) transporters couple hydrolysis of ATP with vectorial transport across the cell membrane. We have reconstituted ABC transporter MsbA in nanodiscs of various sizes and lipid compositions to test whether ATPase activity is modulated by the properties of the bilayer. ATP hydrolysis rates, Michaelis-Menten parameters, and dissociation constants of substrate analog ATP-γ-S demonstrated that physicochemical properties of the bilayer modulated binding and ATPase activity. This is remarkable when considering that the catalytic unit is located ∼50 from the transmembrane region. Our results validated the use of nanodiscs as an effective tool to reconstitute MsbA in an active catalytic state, and highlighted the close relationship between otherwise distant transmembrane and ATPase modules.

Original languageEnglish
Pages (from-to)3533-3537
Number of pages5
JournalFEBS Letters
Volume585
Issue number22
DOIs
Publication statusPublished - Nov 16 2011
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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