PMID: 10681549Feb 22, 2000

TspO of rhodobacter sphaeroides. A structural and functional model for the mammalian peripheral benzodiazepine receptor

The Journal of Biological Chemistry
A A Yeliseev, Samuel Kaplan


The function and specific structural aspects of the tryptophan-rich sensory protein (TspO) of Rhodobacter sphaeroides 2.4.1 were studied using site-directed mutagenesis involving some 17 different amino acids. The choice of these amino acids changes was dictated from an analysis of the TspO family of proteins derived from the data bases. These studies demonstrated the importance of several highly conserved tryptophan residues in the sensory transduction pathway involving TspO through the proposed binding of an intermediate(s) in the tetrapyrrole biosynthesis pathway. These studies also revealed that the substitution of one or several of the amino acid residues dramatically affected, either directly or indirectly, the levels of TspO in the membranes of R. sphaeroides. Mounting evidence is presented suggesting that TspO normally forms a dimer within the bacterial outer membrane, and the dimer form of TspO may be the active form for TspO function. Because our earlier studies provided us with a functional framework within which to view these amino acid substitutions, we are able to suggest a preliminary model for TspO structure-function. Not only do these studies tell us more about TspO, but they also shed light on the TspO homolog...Continue Reading


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Related Concepts

Biochemical Pathway
Bacterial Proteins
Tissue Membrane
Outer Membrane
Structure-Activity Relationship
Amino Acids, I.V. solution additive
Transcription, Genetic

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