1erd: Difference between revisions
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[[ | ==THE NMR SOLUTION STRUCTURE OF THE PHEROMONE ER-2 FROM THE CILIATED PROTOZOAN EUPLOTES RAIKOVI== | ||
<StructureSection load='1erd' size='340' side='right' caption='[[1erd]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1erd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Euplotes_raikovi Euplotes raikovi]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ERD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ERD FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1erd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1erd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1erd RCSB], [http://www.ebi.ac.uk/pdbsum/1erd PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:7833811</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Euplotes raikovi]] | [[Category: Euplotes raikovi]] | ||
[[Category: Bradshaw, R A.]] | [[Category: Bradshaw, R A.]] | ||
Revision as of 11:22, 24 September 2014
THE NMR SOLUTION STRUCTURE OF THE PHEROMONE ER-2 FROM THE CILIATED PROTOZOAN EUPLOTES RAIKOVI
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