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Toward the functional oligomerization state of tryptophan-rich sensory proteins

Authors :
Markus Zweckstetter
Mariusz Jaremko
Stefan Becker
Lukasz Jaremko
Source :
Protein Science. 23:1154-1160
Publication Year :
2014
Publisher :
Wiley, 2014.

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 A 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.

Details

ISSN :
09618368
Volume :
23
Database :
OpenAIRE
Journal :
Protein Science
Accession number :
edsair.doi...........2b61e2eb93efd99ab6bc8fb6171e86ad