The structure of the TOM core complex in the mitochondrial outer membrane

Thomas Bausewein 1 , Hammad Naveed 2 , Jie Liang 3  and Stephan Nussbergerhttp://orcid.org/https://orcid.org/0000-0003-3619-4452 4
  • 1 Max-Planck-Institute of Biophysics, Department of Structural Biology, Max-von-Laue-Str. 3, D-60438Frankfurt am Main, Germany
  • 2 National University of Computer and Emerging Sciences, Department of Computer Science, A. K. Brohi Road H-11/4, Islamabad 44000, Pakistan
  • 3 Richard and Loan Hill Department of Bioengineering, MC-063, University of Illinois, Chicago, IL 60607-7052, USA
  • 4 University of Stuttgart, Institute of Biomaterials and Biomolecular Systems, Department of Biophysics, Pfaffenwaldring 57, D-70569Stuttgart, Germany
Thomas Bausewein
  • Max-Planck-Institute of Biophysics, Department of Structural Biology, Max-von-Laue-Str. 3, D-60438Frankfurt am Main, Germany
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, Hammad Naveed
  • National University of Computer and Emerging Sciences, Department of Computer Science, A. K. Brohi Road H-11/4, Islamabad 44000, Pakistan
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, Jie Liang
  • Richard and Loan Hill Department of Bioengineering, MC-063, University of Illinois, Chicago, IL 60607-7052, USA
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and Stephan NussbergerORCID iD: https://orcid.org/0000-0003-3619-4452

Abstract

In the past three decades, significant advances have been made in providing the biochemical background of TOM (translocase of the outer mitochondrial membrane)-mediated protein translocation into mitochondria. In the light of recent cryoelectron microscopy-derived structures of TOM isolated from Neurospora crassa and Saccharomyces cerevisiae, the interpretation of biochemical and biophysical studies of TOM-mediated protein transport into mitochondria now rests on a solid basis. In this review, we compare the subnanometer structure of N. crassa TOM core complex with that of yeast. Both structures reveal remarkably well-conserved symmetrical dimers of 10 membrane protein subunits. The structural data also validate predictions of weakly stable regions in the transmembrane β-barrel domains of the protein-conducting subunit Tom40, which signal the existence of β-strands located in interfaces of protein-protein interactions.

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