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Data availability
The structural restraints and coordinates have been deposited in the Protein Data Bank (PDB: 7CLV). The chemical shift values have been deposited in the Biological Magnetic Resonance Data Bank (36365).
References
Chacinska, A., Koehler, C. M., Milenkovic, D., Lithgow, T. & Pfanner, N. Cell 138, 628–644 (2009).
Truscott, K. N. et al. Nat. Struct. Mol. Biol. 8, 1074–1082 (2001).
Donzeau, M. et al. Cell 101, 401–412 (2000).
Ting, S., Yan, N. L., Schilke, B. A. & Craig, E. A. Elife 6, e23609 (2017).
Günsel, U. et al. J. Mol. Biol. 432, 3326–3337 (2020).
Demishtein-Zohary, K., Marom, M., Neupert, W., Mokranjac, D. & Azem, A. FEBS J. 282, 2178–2186 (2015).
Alder, N. N., Jensen, R. E. & Johnson, A. E. Cell 134, 439–450 (2008).
Malhotra, K., Sathappa, M., Landin, J. S., Johnson, A. E. & Alder, N. N. Nat. Struct. Mol. Biol. 20, 965–972 (2013).
Yamamoto, H. et al. Cell 111, 519–528 (2002).
Bauer, M. F., Sirrenberg, C., Neupert, W. & Brunner, M. Cell 87, 33–41 (1996).
Liu, Q., D’Silva, P., Walter, W., Marszalek, J. & Craig, E. A. Science 300, 139–141 (2003).
Acknowledgements
We acknowledge the High Magnetic Field Laboratory of Chinese Academy of Sciences and the Biomolecular Magnetic Resonance Center supported by Hesse State at University of Frankfurt for allowing us to access NMR spectrometers. A portion of this work was supported by the High Magnetic Field Laboratory of Anhui Province. This study was supported by grants from the Ministry of Science and Technology of China (Grant No., 2016YFA0400901), the National Natural Science Foundation of China (Grant No., U1632274), Hefei Science Center of Chinese Academy of Sciences (Grant No., 2020HSC-CIP011) and by iNEXT-Discovery, project number 871037, funded by the Horizon 2020 program of the European Commission.
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M.R. purified the NMR samples. S.Z., M.R., Y.L., J.Y., and C.R. performed the NMR experiments and analyzed the NMR data, S.Z. and M.R. determined the NMR structure. B.S. and S.B. performed the electrophysiological experiments. S.Z., H.S., C.X., and J.W. designed the experiments, analyzed the data and wrote the manuscript.
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Zhou, S., Ruan, M., Li, Y. et al. Solution structure of the voltage-gated Tim23 channel in complex with a mitochondrial presequence peptide. Cell Res 31, 821–824 (2021). https://doi.org/10.1038/s41422-020-00452-y
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DOI: https://doi.org/10.1038/s41422-020-00452-y
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