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Toward the functional oligomerization state of tryptophan‐rich sensory proteins
Author(s) -
Jaremko Łukasz,
Jaremko Mariusz,
Becker Stefan,
Zweckstetter Markus
Publication year - 2014
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.2487
Subject(s) - translocator protein , protein quaternary structure , chemistry , biochemistry , biophysics , mutagenesis , tryptophan , heme , rhodobacter sphaeroides , protein structure , biology , mutation , amino acid , protein subunit , photosynthesis , gene , neuroinflammation , immunology , inflammation , enzyme
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.