Fig. 4

Predicted 3D structure of representative EPDRs. a-c; three different views of Capsaspora owczarzaki 30864 (clade 1, profile 1, gold), Saccoglossus kowalevskii 291225509 (clade 2, profile 2, blue) and Naegleria gruberi EFC42264 (clade 2, profile 3, pink) EPDR sequences, superimposed. All three sequences are predicted to form a twisted beta-sheet structure that surrounds a central pocket (visible in C). d. Surface rendering of C, based on the S. kowalevskii sequence. The shading in the centre indicates the location of the pocket. Panels E-J present individual predicted 3D structures of C. owczarzaki 30864 (e), S. kowalevskii 291225509 (f), N. gruberi EFC42264 (g), Danio rerio 134034 (a fish brain ependymin; h), Chaetosphaeridium globosum HO349164 (i), and Aplysia californica (j), respectively, in a similar orientation. Highly conserved cysteine residues are indicated in green. The highly conserved proline (position 150 of alignment) is located at the bottom of the pocket and is indicated in yellow, except for D. rerio 134034 in which it is absent. Predicted glycosylation sites are indicated in red. All sequences display similar predicted structures, however there appears to be some divergence in the portion of the protein distal to the pocket (left of figure), particularly in profile 3 proteins