1erp
From Proteopedia
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1erp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1erp OCA], [http://www.ebi.ac.uk/pdbsum/1erp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1erp RCSB]</span> | ||
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[[Category: pheromone]] | [[Category: pheromone]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:08:23 2008'' |
Revision as of 17:08, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NUCLEAR MAGNETIC RESONANCE SOLUTION STRUCTURE OF THE PHEROMONE ER-10 FROM THE CILIATED PROTOZOAN EUPLOTES RAIKOVI
Overview
The three-dimensional structure in solution of the pheromone Er-10 from the ciliated protozoan Euplotes raikovi has been determined by nuclear magnetic resonance spectroscopy. The structure of this 38-residue protein was obtained from 384 nuclear Overhauser enhancement distance constraints and 78 dihedral angle constraints using the distance geometry program DIANA for the structure calculation and the program AMBER for energy minimization. For a group of 20 conformers used to characterize the solution conformation, the average root-mean-square distance calculated for the backbone heavy atoms relative to the mean structure was 0.33 A. The structure includes three short helices of residues 2 to 8, 12 to 19 and 24 to 33, and a turn in the carboxy-terminal region of residues 34 to 38. These structural elements are held together by three disulfide bridges. The structure is quite stable relative to heat denaturation, since at both pH 4.6 and pH 6.0 only minor changes in the circular dichroism and nuclear magnetic resonance spectra were observed over the temperature range 20 to 80 degrees C. The surface of the Er-10 structure shows an asymmetric charge distribution that results in a predominantly apolar surface on one side of the molecule. There is also a deep cleft in the structure with an asymmetric distribution of charged and apolar residues on the two walls. These surface features may be important for the homologous (autocrine) and heterologous binding of the pheromone to receptors.
About this Structure
1ERP is a Single protein structure of sequence from Euplotes raikovi. Full crystallographic information is available from OCA.
Reference
Nuclear magnetic resonance solution structure of the pheromone Er-10 from the ciliated protozoan Euplotes raikovi., Brown LR, Mronga S, Bradshaw RA, Ortenzi C, Luporini P, Wuthrich K, J Mol Biol. 1993 Jun 5;231(3):800-16. PMID:8515452
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