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Molecular Biophysics
1 Results
- Protein Structure and FoldingOpen Access
Evidence of Distinct Channel Conformations and Substrate Binding Affinities for the Mitochondrial Outer Membrane Protein Translocase Pore Tom40
Journal of Biological ChemistryVol. 290Issue 43p26204–26217Published online: September 2, 2015- Adam J. Kuszak
- Daniel Jacobs
- Philip A. Gurnev
- Takuya Shiota
- John M. Louis
- Trevor Lithgow
- and others
Cited in Scopus: 21Background: Nearly all nascent mitochondrial proteins are transported by the translocase of the outer membrane (TOM) complex.Results: The core Tom40 β-barrel domain exhibits four conductive levels and three distinct substrate binding affinities.Conclusion: Tom40 interactions with presequence substrates depend upon the channel's conformation.Significance: Conformational rearrangements in Tom40 may regulate substrate interactions.