Toward the functional oligomerization state of tryptophan-rich sensory proteins

Łukasz Jaremko, Mariusz Jaremko, Stefan Becker, Markus Zweckstetter*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)1154-1160
Number of pages7
JournalProtein Science
Volume23
Issue number8
DOIs
StatePublished - Aug 2014

Keywords

  • Membrane protein
  • Mitochondria
  • Oligomerization
  • Receptor
  • Structure

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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