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Cryo-EM Structure of the TOM Core Complex from Neurospora crassa.
Bausewein, Thomas; Mills, Deryck J; Langer, Julian D; Nitschke, Beate; Nussberger, Stephan; Kühlbrandt, Werner.
Afiliación
  • Bausewein T; Department of Structural Biology, Max-Planck-Institute of Biophysics, Max-von-Laue-Str. 3, 60438 Frankfurt am Main, Germany.
  • Mills DJ; Department of Structural Biology, Max-Planck-Institute of Biophysics, Max-von-Laue-Str. 3, 60438 Frankfurt am Main, Germany.
  • Langer JD; Department of Molecular Membrane Biology, Max-Planck-Institute of Biophysics, Max-von-Laue-Str. 3, 60438 Frankfurt am Main, Germany.
  • Nitschke B; Abt. Biophysik, Institut für Biomaterialien und biomolekulare Systeme, Universität Stuttgart, Pfaffenwaldring 57, 70550 Stuttgart, Germany.
  • Nussberger S; Abt. Biophysik, Institut für Biomaterialien und biomolekulare Systeme, Universität Stuttgart, Pfaffenwaldring 57, 70550 Stuttgart, Germany.
  • Kühlbrandt W; Department of Structural Biology, Max-Planck-Institute of Biophysics, Max-von-Laue-Str. 3, 60438 Frankfurt am Main, Germany. Electronic address: werner.kuehlbrandt@biophys.mpg.de.
Cell ; 170(4): 693-700.e7, 2017 Aug 10.
Article en En | MEDLINE | ID: mdl-28802041
The TOM complex is the main entry gate for protein precursors from the cytosol into mitochondria. We have determined the structure of the TOM core complex by cryoelectron microscopy (cryo-EM). The complex is a 148 kDa symmetrical dimer of ten membrane protein subunits that create a shallow funnel on the cytoplasmic membrane surface. In the core of the dimer, the ß-barrels of the Tom40 pore form two identical preprotein conduits. Each Tom40 pore is surrounded by the transmembrane segments of the α-helical subunits Tom5, Tom6, and Tom7. Tom22, the central preprotein receptor, connects the two Tom40 pores at the dimer interface. Our structure offers detailed insights into the molecular architecture of the mitochondrial preprotein import machinery.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Fúngicas / Proteínas Portadoras / Sistemas de Translocación de Proteínas / Neurospora crassa Idioma: En Revista: Cell Año: 2017 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Estados Unidos
Texto completo
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XML
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Fúngicas / Proteínas Portadoras / Sistemas de Translocación de Proteínas / Neurospora crassa Idioma: En Revista: Cell Año: 2017 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Estados Unidos