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Journal Article

Toward the functional oligomerization state of tryptophan-rich sensory proteins.

MPS-Authors
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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;

External Resource

http://onlinelibrary.wiley.com/doi/10.1002/pro.2487/pdf
(Publisher version)

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Fulltext (public)

2045213.pdf
(Publisher version), 8MB

Supplementary Material (public)

2045213_Suppl.pdf
(Supplementary material), 9MB

Citation

Jaremko, L., Jaremko, M., Becker, S., & Zweckstetter, M. (2014). Toward the functional oligomerization state of tryptophan-rich sensory proteins. Protein Science, 23(8), 1154-1160. doi:10.1002/pro.2487.


Cite as: https://hdl.handle.net/11858/00-001M-0000-001A-0C19-0
Abstract
A conserved family of tryptophan-rich sensory proteins (TspO) mediates the transport of heme degradation intermediates across membranes. In eukaryotes, the homologous mitochondrial translocator protein (TSPO) binds cholesterol and radioligands as monomer. On the basis of the mammalian TSPO structure, bioinformatic analysis, and a 10 Å resolution electron microscopy map of TspO from Rhodobacter sphaeroides, we developed a model of the tertiary and quaternary structure of TspO that is in agreement with available mutagenesis data. Our study provides insight into the conformational basis for the restricted interaction of bacterial TspO with radioligands and the functional oligomerization state of bacterial TspO proteins.