1awy
From Proteopedia
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'''NMR STRUCTURE OF CALCIUM BOUND CONFORMER OF CONANTOKIN G, MINIMIZED AVERAGE STRUCTURE''' | '''NMR STRUCTURE OF CALCIUM BOUND CONFORMER OF CONANTOKIN G, MINIMIZED AVERAGE STRUCTURE''' | ||
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[[Category: Pedersen, L G.]] | [[Category: Pedersen, L G.]] | ||
[[Category: Rigby, A C.]] | [[Category: Rigby, A C.]] | ||
| - | [[Category: | + | [[Category: Calcium bound]] |
| - | [[Category: | + | [[Category: Conantokin g]] |
| - | [[Category: | + | [[Category: Conotoxin]] |
| - | [[Category: | + | [[Category: Gamma-carboxyglutamic acid]] |
| - | [[Category: | + | [[Category: Venom]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:47:27 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 07:47, 2 May 2008
NMR STRUCTURE OF CALCIUM BOUND CONFORMER OF CONANTOKIN G, MINIMIZED AVERAGE STRUCTURE
Overview
Conantokin G is a gamma-carboxyglutamic acid- (Gla-) containing conotoxin isolated from the venom of the marine cone snail Conus geographus. This 17-residue polypeptide, which contains five gamma-carboxyglutamic acid residues, is a N-methyl-d-aspartate- (NMDA-) type glutamate receptor antagonist. To investigate the role of gamma-carboxyglutamic acid in the calcium-induced structural transition of conantokin G, we determined the three-dimensional structure of the conantokin G/Ca2+ complex by two-dimensional 1H NMR spectroscopy and compared it to the high-resolution structure of conantokin G in the absence of metal ions [Rigby et al. (1997) Biochemistry 36, 6906]. Complete resonance assignments were made by two dimensional 1H NMR spectroscopy at pH 5.6 in the presence of saturating amounts of Ca2+. Distance geometry and simulated annealing methods were used to derive 23 convergent structures from a set of 302 interproton distance restraints and two torsion angle measurements. A high-resolution structure, with the backbone root mean square deviation to the geometric average of the 23 structures of 0.6 +/- 0.1 A, contains a linear alpha-helix from Gla 3 to Lys 15. Gla residues 3, 7, 10, and 14 are aligned in a linear array on one face of the helix. A genetic algorithm was applied to determine the calcium positions in conantokin G, and the conantokin G/Ca2+ complex refined by molecular simulation. Upon binding of Ca2+ to gamma-carboxyglutamic acid, conantokin G undergoes a conformational transition from a distorted curvilinear 310 helix to a linear alpha-helix. Occupancy of the metal binding sites, defined by gamma-carboxyglutamic acids, results in formation of a calcium-carboxylate network that linearizes the helix and exposes the hydrophobic amino acids on the opposite face of the helix.
About this Structure
1AWY is a Single protein structure of sequence from Conus geographus. Full crystallographic information is available from OCA.
Reference
Role of gamma-carboxyglutamic acid in the calcium-induced structural transition of conantokin G, a conotoxin from the marine snail Conus geographus., Rigby AC, Baleja JD, Li L, Pedersen LG, Furie BC, Furie B, Biochemistry. 1997 Dec 16;36(50):15677-84. PMID:9398296 Page seeded by OCA on Fri May 2 10:47:27 2008
