5O8O
N. crassa Tom40 model based on cryo-EM structure of the TOM core complex at 6.8 A
Summary for 5O8O
| Entry DOI | 10.2210/pdb5o8o/pdb |
| EMDB information | 3761 |
| Descriptor | Mitochondrial import receptor subunit tom40 (1 entity in total) |
| Functional Keywords | tom-complex, protein import, mitochondria, cryo-em, protein transport |
| Biological source | Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
| Total number of polymer chains | 1 |
| Total formula weight | 38184.80 |
| Authors | Bausewein, T.,Mills, D.J.,Nussberger, S.,Nitschke, B.,Kuehlbrandt, W. (deposition date: 2017-06-13, release date: 2017-08-16, Last modification date: 2024-05-15) |
| Primary citation | Bausewein, T.,Mills, D.J.,Langer, J.D.,Nitschke, B.,Nussberger, S.,Kuhlbrandt, W. Cryo-EM Structure of the TOM Core Complex from Neurospora crassa. Cell, 170:693-700.e7, 2017 Cited by PubMed 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. PubMed: 28802041DOI: 10.1016/j.cell.2017.07.012 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (6.8 Å) |
Structure validation
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