1erd

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THE NMR SOLUTION STRUCTURE OF THE PHEROMONE ER-2 FROM THE CILIATED PROTOZOAN EUPLOTES RAIKOVI

Overview

The NMR structure of the pheromone Er-2 from the ciliated protozoan, Euplotes raikovi has been determined in aqueous solution. The structure of, this 40-residue protein was calculated with the distance geometry program, DIANA from 621 distance constraints and 89 dihedral angle constraints; the, program OPAL was employed for the energy minimization. For a group of 20, conformers used to characterize the solution structure, the average, pairwise RMS deviation from the mean structure calculated for the backbone, heavy atoms N, C alpha, and C' of residues 3-37 was 0.31 A. The molecular, architecture is dominated by an up-down-up bundle of 3 short helices of, residues 5-11, 14-20, and 23-33, which is similar to the structures of the, homologous pheromones Er-1 and Er-10. Novel structural features include a, well-defined N-cap on the first helix, a 1-residue deletion in the second, helix resulting in the formation of a 3(10)-helix rather than an, alpha-helix as found in Er-1 and Er-10, and the simultaneous presence of 2, different conformations for the C-terminal tetrapeptide segment, i.e., a, major conformation with the Leu 39-Pro 40 peptide bond in the trans form, and a minor conformation with this peptide bond in the cis form.

About this Structure

1ERD is a Single protein structure of sequence from Euplotes raikovi. Full crystallographic information is available from OCA.

Reference

The NMR solution structure of the pheromone Er-2 from the ciliated protozoan Euplotes raikovi., Ottiger M, Szyperski T, Luginbuhl P, Ortenzi C, Luporini P, Bradshaw RA, Wuthrich K, Protein Sci. 1994 Sep;3(9):1515-26. PMID:7833811

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