Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous AbstractFlavor of cold-hardy grapes: impact of berry maturity and environmental conditions    Next Abstract"Molecular Structures and Coding Genes of the Water-Borne Protein Pheromones of Euplotes petzi, an Early Diverging Polar Species of Euplotes" »

J Mol Biol


Title:Cold-adaptation in sea-water-borne signal proteins: sequence and NMR structure of the pheromone En-6 from the Antarctic ciliate Euplotes nobilii
Author(s):Pedrini B; Placzek WJ; Koculi E; Alimenti C; LaTerza A; Luporini P; Wuthrich K;
Address:"Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA"
Journal Title:J Mol Biol
Year:2007
Volume:20070626
Issue:2
Page Number:277 - 286
DOI: 10.1016/j.jmb.2007.06.046
ISSN/ISBN:0022-2836 (Print) 0022-2836 (Linking)
Abstract:"Ciliates of Euplotes species constitutively secrete pleiotropic protein pheromones, which are capable to function as prototypic autocrine growth factors as well as paracrine inducers of mating processes. This paper reports the amino acid sequence and the NMR structure of the pheromone En-6 isolated from the antarctic species Euplotes nobilii. The 63-residue En-6 polypeptide chain forms three alpha-helices in positions 18-25, 36-40 and 46-56, which are arranged in an up-down-up three-helix bundle forming the edges of a distorted trigonal pyramid. The base of the pyramid is covered by the N-terminal heptadecapeptide segment, which includes a 3(10)-turn of residues 3-6. This topology is covalently anchored by four long-range disulfide bonds. Comparison with the smaller pheromones of E. raikovi, a closely related species living in temperate waters, shows that the two-pheromone families have the same three-helix bundle architecture. It then appears that cold-adaptation of the En proteins is primarily related to increased lengths of the chain-terminal peptide segments and the surface-exposed loops connecting the regular secondary structures, and to the presence of solvent-exposed clusters of negatively charged side-chains"
Keywords:"*Acclimatization Amino Acid Sequence Animals Antarctic Regions *Cold Temperature Disulfides/chemistry/metabolism Euplotes/*chemistry Models, Molecular Molecular Sequence Data *Nuclear Magnetic Resonance, Biomolecular Pheromones/*chemistry/isolation & puri;"
Notes:"MedlinePedrini, Bill Placzek, William J Koculi, Eda Alimenti, Claudio LaTerza, Antonietta Luporini, Pierangelo Wuthrich, Kurt eng Research Support, Non-U.S. Gov't Netherlands 2007/07/31 J Mol Biol. 2007 Sep 14; 372(2):277-86. doi: 10.1016/j.jmb.2007.06.046. Epub 2007 Jun 26"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 22-11-2024