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Independent saturation of three TrpRS subsites generates a partially assembled state similar to those observed in molecular simulations

Abstract : Two new crystal structures of Bacillus stearothermophilus tryptophanyl-tRNA synthetase (TrpRS) afford evidence that a closed interdomain hinge angle requires a covalent bond between AMP and an occupant of either pyrophosphate or tryptophan subsite. They also are within experimental error of a cluster of structures observed in a nonequilibrium molecular dynamics simulation showing partial active-site assembly. Further, the highest energy structure in a minimum action pathway computed by using elastic network models for Open and Pretransition state (PreTS) conformations for the fully liganded TrpRS monomer is intermediate between that simulated structure and a partially disassembled structure from a nonequilibrium molecular dynamics trajectory for the unliganded PreTS. These mutual consistencies provide unexpected validation of inferences drawn from molecular simulations.
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Submitted on : Friday, July 5, 2019 - 12:49:10 PM
Last modification on : Tuesday, May 31, 2022 - 10:20:16 AM

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Poramaet Laowanapiban, Maryna Kapustina, Clemens Vonrhein, Marc Delarue, Patrice Koehl, et al.. Independent saturation of three TrpRS subsites generates a partially assembled state similar to those observed in molecular simulations. Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2009, 106 (6), pp.1790-1795. ⟨10.1073/pnas.0812752106⟩. ⟨pasteur-02174885⟩

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