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TitleCryo-EM Structure of the TOM Core Complex from Neurospora crassa.
Journal, issue, pagesCell, Vol. 170, Issue 4, Page 693-700.e7, Year 2017
Publish dateAug 10, 2017
AuthorsThomas Bausewein / Deryck J Mills / Julian D Langer / Beate Nitschke / Stephan Nussberger / Werner Kühlbrandt /
PubMed AbstractThe 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 ...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 β-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.
External linksCell / PubMed:28802041
MethodsEM (single particle)
Resolution6.8 Å
Structure data

3761

5o8o

EMDB-3761: Cryo-EM structure of the TOM core complex from Neurospora crassa
PDB-5o8o: N. crassa Tom40 model based on cryo-EM structure of the TOM core complex at 6.8 A
Method: EM (single particle) / Resolution: 6.8 Å

Source
  • Neurospora crassa (fungus)
  • neurospora crassa (strain atcc 24698 / 74-or23-1a / cbs 708.71 / dsm 1257 / fgsc 987) (fungus)
KeywordsPROTEIN TRANSPORT / TOM-Complex / Protein Import / Mitochondria / Cryo-EM

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