1jyt

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1jyt

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Solution structure of olfactory marker protein from rat

Overview

Olfactory marker protein (OMP) is a ubiquitous, cytoplasmic protein found, in mature olfactory receptor neurons of all vertebrates., Electrophysiological and behavioral studies demonstrate that it is a, modulator of the olfactory signal transduction pathway. Here, we, demonstrate that the solution structure of OMP, as determined by NMR, studies, is a single globular domain protein comprised of eight, beta-strands forming two beta-sheets oriented orthogonally to one another, thus exhibiting a "beta-clam" or "beta-sandwich" fold: beta-sheet 1 is, comprised of beta3-beta8-beta1-beta2 and beta-sheet 2 contains, beta6-beta5-beta4-beta7. Insertions include two, long alpha-helices, located on opposite sides of the beta-clam and three flexible loops. The, juxtaposition of beta-strands, beta6-beta5-beta4-beta7-beta2-beta1-beta8-beta3 forms a continuously, curved surface and encloses one side of the beta-clam. The "cleft" formed, by the two beta-sheets is opposite to the closed end of the beta-clam., Using a peptide titration series, we have identified this cleft as the, binding surface for a peptide derived from the Bex1 protein. The highly, conserved Omega-loop structure adjacent to the Bex1 peptide-binding, surface found in OMP may be the site of additional OMP-protein, interactions related to its role in modulating olfactory signal, transduction. Thus, the interaction between the OMP and Bex1 proteins, could facilitate the interaction between OMP and other components of the, olfactory signaling pathway.

About this Structure

1JYT is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Olfactory marker protein (OMP) exhibits a beta-clam fold in solution: implications for target peptide interaction and olfactory signal transduction., Baldisseri DM, Margolis JW, Weber DJ, Koo JH, Margolis FL, J Mol Biol. 2002 Jun 7;319(3):823-37. PMID:12054873

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