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Fig. 7 | BMC Molecular and Cell Biology

Fig. 7

From: Design and structural characterisation of olfactomedin-1 variants as tools for functional studies

Fig. 7

Crystal structure of dimeric recombinant Olfm1coil-Olf with bound Na+ and Ca2+ ions. a Crystal structure of Olfm1coil-Olf with bound Na+ (purple) and Ca2+ (green) and the switch loop in violet. Disulfides are indicated as spheres and N-linked glycans as brown sticks. b Comparison of the previously-solved limited proteolysis fragment of Olfm1coil-Olf in the apo state (teal, PDB 5AMO) with the presented structure in the Na+- and Ca2+-bound state (orange) shows a very similar structure (Cα RMSD of 0.73 Å), except for the switch loop that is structured in the Na+- and Ca2+-bound state (it is unstructured in the apo state). c Surface representation of Olfm1coil-Olf with the putative conditional interface formed by the switch loop (violet). d Conservation of Olfm1 amongst vertebrate orthologues plotted on the surface using Consurf [53]. The contour of the switch loop interface as in c is indicated with a yellow line. Both the top face of the β-propellers (indicated with an accolade in the left panel; front view in the right panel) and the crevice between the two Olf domains (indicated with an ellipse in the bottom panel) are highly conserved and may be interfaces for protein-protein interaction

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