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Structural insight into mitochondrial ß-barrel outer membrane protein biogenesis.
Diederichs, Kathryn A; Ni, Xiaodan; Rollauer, Sarah E; Botos, Istvan; Tan, Xiaofeng; King, Martin S; Kunji, Edmund R S; Jiang, Jiansen; Buchanan, Susan K.
Afiliação
  • Diederichs KA; Laboratory of Molecular Biology, National Institute of Diabetes & Digestive & Kidney Diseases, National Institutes of Health, 9000 Rockville Pike, Bethesda, MD, 20892, USA.
  • Ni X; Laboratory of Membrane Proteins and Structural Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, 20892, USA.
  • Rollauer SE; Laboratory of Molecular Biology, National Institute of Diabetes & Digestive & Kidney Diseases, National Institutes of Health, 9000 Rockville Pike, Bethesda, MD, 20892, USA.
  • Botos I; MRC Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge, CB2 0XY, UK.
  • Tan X; Vertex Pharmaceuticals, 50 Northern Avenue, Boston, MA, 02210, USA.
  • King MS; Laboratory of Molecular Biology, National Institute of Diabetes & Digestive & Kidney Diseases, National Institutes of Health, 9000 Rockville Pike, Bethesda, MD, 20892, USA.
  • Kunji ERS; Laboratory of Membrane Proteins and Structural Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, 20892, USA.
  • Jiang J; MRC Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge, CB2 0XY, UK.
  • Buchanan SK; MRC Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge, CB2 0XY, UK.
Nat Commun ; 11(1): 3290, 2020 07 03.
Article em En | MEDLINE | ID: mdl-32620929
In mitochondria, ß-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 ß-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 ß-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 ß-barrel opens a lateral gate to accommodate its substrates.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Saccharomyces cerevisiae / Biossíntese de Proteínas / Proteínas de Transporte da Membrana Mitocondrial / Membranas Mitocondriais / Mitocôndrias Idioma: En Ano de publicação: 2020 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Saccharomyces cerevisiae / Biossíntese de Proteínas / Proteínas de Transporte da Membrana Mitocondrial / Membranas Mitocondriais / Mitocôndrias Idioma: En Ano de publicação: 2020 Tipo de documento: Article