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Journal articles
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.
https://hal-pasteur.archives-ouvertes.fr/pasteur-02174885
Contributor : Marie de Tarragon Connect in order to contact the contributor
Submitted on : Friday, July 5, 2019 - 12:49:10 PM
Last modification on : Tuesday, October 19, 2021 - 10:26:39 PM
Contributor : Marie de Tarragon Connect in order to contact the contributor
Submitted on : Friday, July 5, 2019 - 12:49:10 PM
Last modification on : Tuesday, October 19, 2021 - 10:26:39 PM
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