1erd
From Proteopedia
(New page: 200px<br /><applet load="1erd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1erd" /> '''THE NMR SOLUTION STRUCTURE OF THE PHEROMONE ...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1erd.gif|left|200px]]<br /><applet load="1erd" size=" | + | [[Image:1erd.gif|left|200px]]<br /><applet load="1erd" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1erd" /> | caption="1erd" /> | ||
'''THE NMR SOLUTION STRUCTURE OF THE PHEROMONE ER-2 FROM THE CILIATED PROTOZOAN EUPLOTES RAIKOVI'''<br /> | '''THE NMR SOLUTION STRUCTURE OF THE PHEROMONE ER-2 FROM THE CILIATED PROTOZOAN EUPLOTES RAIKOVI'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The NMR structure of the pheromone Er-2 from the ciliated protozoan | + | 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== | ==About this Structure== | ||
| - | 1ERD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Euplotes_raikovi Euplotes raikovi]. Full crystallographic information is available from [http:// | + | 1ERD is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
| Line 13: | Line 13: | ||
[[Category: Euplotes raikovi]] | [[Category: Euplotes raikovi]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bradshaw, R | + | [[Category: Bradshaw, R A.]] |
[[Category: Luginbuhl, P.]] | [[Category: Luginbuhl, P.]] | ||
[[Category: Luporini, P.]] | [[Category: Luporini, P.]] | ||
| Line 22: | Line 22: | ||
[[Category: pheromone]] | [[Category: pheromone]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:30:48 2008'' |
Revision as of 10:30, 21 February 2008
|
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
Page seeded by OCA on Thu Feb 21 12:30:48 2008
