The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Cryo-EM structure of the mitochondrial protein-import channel TOM complex at near-atomic resolution
Open accessAbstract
Nearly all mitochondrial proteins are encoded by the nuclear genome and imported into mitochondria after synthesis on cytosolic ribosomes. These precursor proteins are translocated into mitochondria by the TOM complex, a protein-conducting channel in the mitochondrial outer membrane. We have determined high-resolution cryo-EM structures of the core TOM complex from Saccharomyces cerevisiae in dimeric and tetrameric forms. Dimeric TOM consists of two copies each of five proteins arranged in two-fold symmetry: pore-forming β-barrel protein Tom40 and four auxiliary α-helical transmembrane proteins. The pore of each Tom40 has an overall negatively charged inner surface attributed to multiple functionally important acidic patches. The tetrameric complex is essentially a dimer of dimeric TOM, which may be capable of forming higher-order oligomers. Our study reveals the detailed molecular organization of the TOM complex and provides new insights about the mechanism of protein translocation into mitochondria. High-resolution cryo-EM structures of the core TOM complex from Saccharomyces cerevisiae, as dimeric and tetrameric assemblies, provide new insights into the mechanism of protein translocation into mitochondria.
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MolProbity : all-atom structure validation for macromolecular crystallography
Chen, V. B., Arendall, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S., & Richardson, D. C. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909042073 · Cited by 14,115
Exploration of Essential Gene Functions via Titratable Promoter Alleles
Mnaimneh, S., Davierwala, A. P., Haynes, J., Moffat, J., Peng, W.-T., Zhang, W., Yang, X., Pootoolal, J., Chua, G., Lopez, A., et al. (2004) · Cell · doi:10.1016/j.cell.2004.06.013 · Cited by 604
Proteomic analysis of the mouse liver mitochondrial inner membrane
Da Cruz, S., Xenarios, I., Langridge, J., Vilbois, F., Parone, P. A., & Martinou, J.-C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304940200 · Cited by 247
Roles of Tom70 in Import of Presequence-containing Mitochondrial Proteins
Yamamoto, H., Fukui, K., Takahashi, H., Kitamura, S., Shiota, T., Terao, K., Uchida, M., Esaki, M., Nishikawa, S.-I., Yoshihisa, T., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.041756 · Cited by 119
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Structure of human PINK1 at a mitochondrial TOM-VDAC array
Callegari, S., Kirk, N. S., Gan, Z. Y., Dite, T., Cobbold, S. A., Leis, A., Dagley, L. F., Glukhova, A., & Komander, D. (2025) · Science · doi:10.1126/science.adu6445 · Cited by 75
Molecular pathway of mitochondrial preprotein import through the TOM–TIM23 supercomplex
Zhou, X., Yang, Y., Wang, G., Wang, S., Sun, D., Ou, X., Lian, Y., & Li, L. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01103-7 · Cited by 72
Lipid scrambling is a general feature of protein insertases
Li, D., Rocha-Roa, C., Schilling, M. A., Reinisch, K. M., & Vanni, S. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2319476121 · Cited by 63
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Metadata
- Authors
- Tucker, K., & Park, E.
- Venue
- Nature Structural & Molecular Biology
- Published
- 2019-11-18
- Volume
- 26
- Issue
- 12
- Pages
- 1158-1166
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W2989453214
- Cited by
- 180
- References
- 4
- FWCI
- 6.87
- Type
- journal article
- Language
- en
- Open access
- green
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