1f35
From Proteopedia
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CRYSTAL STRUCTURE OF MURINE OLFACTORY MARKER PROTEIN
Overview
Olfactory marker protein (OMP) is a highly expressed and phylogenetically, conserved cytoplasmic protein of unknown function found almost exclusively, in mature olfactory sensory neurons. Electrophysiological studies of, olfactory epithelia in OMP knock-out mice show strongly retarded recovery, following odorant stimulation leading to an impaired response to pulsed, odor stimulation. Although these studies show that OMP is a modulator of, the olfactory signal-transduction cascade, its biochemical role is not, established. In order to facilitate further studies on the molecular, function of OMP, its crystal structure has been determined at 2.3 A, resolution using multiwavelength anomalous diffraction experiments on, selenium-labeled protein. OMP is observed to form a modified, beta-clamshell structure with eight antiparallel beta-strands. While OMP, has no significant sequence homology to proteins of known structure, it, has a similar fold to a domain found in a variety of existing structures, including in a large family of viral capsid proteins. The surface of OMP, is mostly convex and lacking obvious small molecule binding sites, suggesting that it is more likely to be involved in modulating, protein-protein interaction than in interacting with small molecule, ligands. Three highly conserved regions have been identified as leading, candidates for protein-protein interaction sites in OMP. One of these, sites represents a loop known to mediate ligand interactions in the, structurally homologous EphB2 receptor ligand-binding domain. This site is, partially buried in the crystal structure but fully exposed in the NMR, solution structure of OMP due to a change in the orientation of an, alpha-helix that projects outward from the structurally invariant, beta-clamshell core. Gating of this conformational change by molecular, interactions in the signal-transduction cascade could be used to control, access to OMP's equivalent of the EphB2 ligand-interaction loop, thereby, allowing OMP to function as a molecular switch.
About this Structure
1F35 is a Single protein structure of sequence from Mus musculus with ZN and CAC as ligands. Full crystallographic information is available from OCA.
Reference
The crystal structure of the olfactory marker protein at 2.3 A resolution., Smith PC, Firestein S, Hunt JF, J Mol Biol. 2002 Jun 7;319(3):807-21. PMID:12054872
Page seeded by OCA on Tue Nov 20 14:34:06 2007
