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Structural insight into mitochondrial β-barrel outer membrane protein biogenesis

Author

Listed:
  • Kathryn A. Diederichs

    (Laboratory of Molecular Biology, National Institute of Diabetes & Digestive & Kidney Diseases, National Institutes of Health, 9000 Rockville Pike)

  • Xiaodan Ni

    (Laboratory of Membrane Proteins and Structural Biology, National Heart, Lung, and Blood Institute, National Institutes of Health)

  • Sarah E. Rollauer

    (Laboratory of Molecular Biology, National Institute of Diabetes & Digestive & Kidney Diseases, National Institutes of Health, 9000 Rockville Pike
    University of Cambridge, Cambridge Biomedical Campus
    Vertex Pharmaceuticals)

  • Istvan Botos

    (Laboratory of Molecular Biology, National Institute of Diabetes & Digestive & Kidney Diseases, National Institutes of Health, 9000 Rockville Pike)

  • Xiaofeng Tan

    (Laboratory of Membrane Proteins and Structural Biology, National Heart, Lung, and Blood Institute, National Institutes of Health)

  • Martin S. King

    (University of Cambridge, Cambridge Biomedical Campus)

  • Edmund R. S. Kunji

    (University of Cambridge, Cambridge Biomedical Campus)

  • Jiansen Jiang

    (Laboratory of Membrane Proteins and Structural Biology, National Heart, Lung, and Blood Institute, National Institutes of Health)

  • Susan K. Buchanan

    (Laboratory of Molecular Biology, National Institute of Diabetes & Digestive & Kidney Diseases, National Institutes of Health, 9000 Rockville Pike)

Abstract

In mitochondria, β-barrel outer membrane proteins mediate protein import, metabolite transport, lipid transport, and biogenesis. The Sorting and Assembly Machinery (SAM) complex consists of three proteins that assemble as a 1:1:1 complex to fold β-barrel proteins and insert them into the mitochondrial outer membrane. We report cryoEM structures of the SAM complex from Myceliophthora thermophila, which show that Sam50 forms a 16-stranded transmembrane β-barrel with a single polypeptide-transport-associated (POTRA) domain extending into the intermembrane space. Sam35 and Sam37 are located on the cytosolic side of the outer membrane, with Sam35 capping Sam50, and Sam37 interacting extensively with Sam35. Sam35 and Sam37 each adopt a GST-like fold, with no functional, structural, or sequence similarity to their bacterial counterparts. Structural analysis shows how the Sam50 β-barrel opens a lateral gate to accommodate its substrates.

Suggested Citation

  • Kathryn A. Diederichs & Xiaodan Ni & Sarah E. Rollauer & Istvan Botos & Xiaofeng Tan & Martin S. King & Edmund R. S. Kunji & Jiansen Jiang & Susan K. Buchanan, 2020. "Structural insight into mitochondrial β-barrel outer membrane protein biogenesis," Nature Communications, Nature, vol. 11(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-17144-1
    DOI: 10.1038/s41467-020-17144-1
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