Abstract
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.
Keywords:
TOM complex; cryo-EM; mitochondria; protein import.
Copyright © 2017 Elsevier Inc. All rights reserved.
MeSH terms
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Amino Acid Sequence
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Carrier Proteins / chemistry*
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Carrier Proteins / genetics
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Carrier Proteins / ultrastructure
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Cryoelectron Microscopy
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Fungal Proteins / chemistry*
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Fungal Proteins / genetics
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Fungal Proteins / ultrastructure
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Mass Spectrometry
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Mitochondrial Membrane Transport Proteins / chemistry
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Mitochondrial Membrane Transport Proteins / genetics
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Mitochondrial Membrane Transport Proteins / ultrastructure
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Mitochondrial Membranes / enzymology
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Mitochondrial Precursor Protein Import Complex Proteins
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Models, Molecular
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Neurospora crassa / enzymology*
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Protein Conformation, beta-Strand
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Protein Translocation Systems / chemistry*
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Protein Translocation Systems / genetics
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Protein Translocation Systems / ultrastructure
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Saccharomyces cerevisiae Proteins / chemistry
Substances
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Carrier Proteins
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Fungal Proteins
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Mitochondrial Membrane Transport Proteins
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Mitochondrial Precursor Protein Import Complex Proteins
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Protein Translocation Systems
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Saccharomyces cerevisiae Proteins