Molecular basis of the dynamic structure of the TIM23 complex in the 
mitochondrial intermembrane space.

Bajaj, R.; Jaremko, L.; Jaremko, M.; Becker, S.; Zweckstetter, M.

doi:10.1016/j.str.2014.07.015

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Molecular basis of the dynamic structure of the TIM23 complex in the mitochondrial intermembrane space.

MPG-Autoren

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Bajaj, R.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

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Jaremko, L.
Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Jaremko, M.
Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Becker, S.
Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Zweckstetter, M.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

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http://www.sciencedirect.com/science/article/pii/S0969212614002597/pdfft?md5=84bfb128af462cec6deb720b75b2cfc6&pid=1-s2.0-S0969212614002597-main.pdf
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Zitation

Bajaj, R., Jaremko, L., Jaremko, M., Becker, S., & Zweckstetter, M. (2014). Molecular basis of the dynamic structure of the TIM23 complex in the mitochondrial intermembrane space. Structure, 22(10), 1501-1511. doi:10.1016/j.str.2014.07.015.

Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0024-3317-9

Zusammenfassung

The presequence translocase TIM23 is a highly dynamic complex in which its subunits can adopt multiple conformations and undergo association-dissociation to facilitate import of proteins into mitochondria. Despite the importance of protein-protein interactions in TIM23, little is known about the molecular details of these processes. Using nuclear magnetic resonance spectroscopy, we characterized the dynamic interaction network of the intermembrane space domains of Tim23, Tim21, Tim50, and Tom22 at single-residue level. We show that Tim23IMS contains multiple sites to efficiently interact with the intermembrane space domain of Tim21 and to bind to Tim21, Tim50, and Tom22. In addition, we reveal the atomic details of the dynamic Tim23IMS-Tim21IMS complex. The combined data support a central role of the intermembrane space domain of Tim23 in the formation and regulation of the presequence translocase.