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Protein Sci

Title:		The NMR solution structure of the pheromone Er-2 from the ciliated protozoan Euplotes raikovi
Author(s):		Ottiger M; Szyperski T; Luginbuhl P; Ortenzi C; Luporini P; Bradshaw RA; Wuthrich K;
Address:		"Institut fur Molekularbiologie und Biophysik, Eidgenossische Technische Hochschule, Zurich, Switzerland"
Journal Title:		Protein Sci
Year:		1994
Volume:		3
Issue:		9
Page Number:		1515 - 1526
DOI:		10.1002/pro.5560030917
ISSN/ISBN:		0961-8368 (Print) 1469-896X (Electronic) 0961-8368 (Linking)
Abstract:		"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"
Keywords:		"Amino Acid Sequence Animals Computer Simulation Euplotes/*chemistry Magnetic Resonance Spectroscopy Models, Molecular Molecular Sequence Data Pheromones/*chemistry Protein Conformation Protein Structure, Secondary Protozoan Proteins/*chemistry Solutions/c;"
Notes:		"MedlineOttiger, M Szyperski, T Luginbuhl, P Ortenzi, C Luporini, P Bradshaw, R A Wuthrich, K eng DK 32465/DK/NIDDK NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. 1994/09/01 Protein Sci. 1994 Sep; 3(9):1515-26. doi: 10.1002/pro.5560030917"