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Toward the functional oligomerization state of tryptophan‐rich sensory proteins
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AbstractA 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 fromRhodobacter 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.
Title: Toward the functional oligomerization state of tryptophan‐rich sensory proteins
Description:
AbstractA 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 fromRhodobacter 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.
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