Methionyl-tRNA synthetase from E. coli: direct evidence for exchange of protomers in the dimeric enzyme by using deuteration and small-angle neutron scattering.
Direct demonstration of the reversible dissociation of native dimeric methionyl-tRNA synthetase from E. coli has been obtained using small angle neutron scattering and deuterated enzyme. Structural parameters of the fully deuterated dimer are very similar to the hydrogenated one. Analysis of the variations of the intensity and of the radius of gyration of a stoichiometric mixture of the two types of dimer (hydrogenated and deuterated), as a function of D2O content in the solvent, enabled us to characterize an hybrid dimer, having both hydrogenated and deuterated protomers. By separating the contribution of each protomer to the scattering, the radius of gyration of the protomer in situ and the distance between the centers of mass of each protomer in the dimer are determined.
D000604:Amino Acyl-tRNA Synthetases; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003903:Deuterium; D004926:Escherichia coli / Q000201:enzymology*; D046911:Macromolecular Substances; D008718:Methionine-tRNA Ligase; D009502:Neutrons; D012542:Scattering, Radiation
D046911:Macromolecular Substances; D003903:Deuterium; D000604:Amino Acyl-tRNA Synthetases; D008718:Methionine-tRNA Ligase