Structural insight into mitochondrial β-barrel outer membrane protein biogenesis

Kathryn A. Diederichs, Xiaodan Ni, Sarah E. Rollauer, Istvan Botos, Xiaofeng Tan, Martin S. King, Edmund R. S. Kunji, Jiansen Jiang () and Susan K. Buchanan ()
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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
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

Nature Communications, 2020, vol. 11, issue 1, 1-13

Abstract: 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.

Date: 2020
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DOI: 10.1038/s41467-020-17144-1

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