Cryo-EM Structure of the TOM Core Complex from Neurospora crassa - PubMed (original) (raw)
. 2017 Aug 10;170(4):693-700.e7.
doi: 10.1016/j.cell.2017.07.012.
Affiliations
- PMID: 28802041
- DOI: 10.1016/j.cell.2017.07.012
Free article
Cryo-EM Structure of the TOM Core Complex from Neurospora crassa
Thomas Bausewein et al. Cell. 2017.
Free article
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.
Similar articles
- Structural snapshot of the mitochondrial protein import gate.
Araiso Y, Imai K, Endo T. Araiso Y, et al. FEBS J. 2021 Sep;288(18):5300-5310. doi: 10.1111/febs.15661. Epub 2020 Dec 26. FEBS J. 2021. PMID: 33305524 - Structure of the mitochondrial import gate reveals distinct preprotein paths.
Araiso Y, Tsutsumi A, Qiu J, Imai K, Shiota T, Song J, Lindau C, Wenz LS, Sakaue H, Yunoki K, Kawano S, Suzuki J, Wischnewski M, Schütze C, Ariyama H, Ando T, Becker T, Lithgow T, Wiedemann N, Pfanner N, Kikkawa M, Endo T. Araiso Y, et al. Nature. 2019 Nov;575(7782):395-401. doi: 10.1038/s41586-019-1680-7. Epub 2019 Oct 10. Nature. 2019. PMID: 31600774 - Tom40, the pore-forming component of the protein-conducting TOM channel in the outer membrane of mitochondria.
Ahting U, Thieffry M, Engelhardt H, Hegerl R, Neupert W, Nussberger S. Ahting U, et al. J Cell Biol. 2001 Jun 11;153(6):1151-60. doi: 10.1083/jcb.153.6.1151. J Cell Biol. 2001. PMID: 11402060 Free PMC article. - The structure of the TOM core complex in the mitochondrial outer membrane.
Bausewein T, Naveed H, Liang J, Nussberger S. Bausewein T, et al. Biol Chem. 2020 May 26;401(6-7):687-697. doi: 10.1515/hsz-2020-0104. Biol Chem. 2020. PMID: 32142473 Review. - Role of the TOM Complex in Protein Import into Mitochondria: Structural Views.
Araiso Y, Imai K, Endo T. Araiso Y, et al. Annu Rev Biochem. 2022 Jun 21;91:679-703. doi: 10.1146/annurev-biochem-032620-104527. Epub 2022 Mar 14. Annu Rev Biochem. 2022. PMID: 35287471 Review.
Cited by
- Biogenesis of mitochondrial β-barrel membrane proteins.
Ganesan I, Busto JV, Pfanner N, Wiedemann N. Ganesan I, et al. FEBS Open Bio. 2024 Oct;14(10):1595-1609. doi: 10.1002/2211-5463.13905. Epub 2024 Sep 29. FEBS Open Bio. 2024. PMID: 39343721 Free PMC article. Review. - Structure of the intact Tom20 receptor in the human translocase of the outer membrane complex.
Su J, Tian X, Wang Z, Yang J, Sun S, Sui SF. Su J, et al. PNAS Nexus. 2024 Jul 26;3(7):pgae269. doi: 10.1093/pnasnexus/pgae269. eCollection 2024 Jul. PNAS Nexus. 2024. PMID: 39071881 Free PMC article. - New insights into the structure and dynamics of the TOM complex in mitochondria.
Nussberger S, Ghosh R, Wang S. Nussberger S, et al. Biochem Soc Trans. 2024 Apr 24;52(2):911-922. doi: 10.1042/BST20231236. Biochem Soc Trans. 2024. PMID: 38629718 Free PMC article. Review. - Tracking the Activity and Position of Mitochondrial β-Barrel Proteins.
Wang S, Nussberger S. Wang S, et al. Methods Mol Biol. 2024;2778:221-236. doi: 10.1007/978-1-0716-3734-0_14. Methods Mol Biol. 2024. PMID: 38478281 - Modular Assembly of Mitochondrial β-Barrel Proteins.
Bhowmik R, den Brave F, Becker T. Bhowmik R, et al. Methods Mol Biol. 2024;2778:201-220. doi: 10.1007/978-1-0716-3734-0_13. Methods Mol Biol. 2024. PMID: 38478280
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources