1erd: Difference between revisions
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'''THE NMR SOLUTION STRUCTURE OF THE PHEROMONE ER-2 FROM THE CILIATED PROTOZOAN EUPLOTES RAIKOVI''' | {{Structure | ||
|PDB= 1erd |SIZE=350|CAPTION= <scene name='initialview01'>1erd</scene> | |||
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'''THE NMR SOLUTION STRUCTURE OF THE PHEROMONE ER-2 FROM THE CILIATED PROTOZOAN EUPLOTES RAIKOVI''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1ERD is a [ | 1ERD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Euplotes_raikovi Euplotes raikovi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ERD OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/7833811 7833811] | ||
[[Category: Euplotes raikovi]] | [[Category: Euplotes raikovi]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: pheromone]] | [[Category: pheromone]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:59:17 2008'' | ||
Revision as of 08:59, 20 March 2008
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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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