Poramaet LaowanapibanMaryna KapustinaClemens VonrheinMarc DelaruePatrice KoehlCharles W. CarterThe University of North Carolina at Chapel HillGlobal Phasing LtdCNRS Centre National de la Recherche ScientifiqueUniversity of California, DavisMahidol University2018-09-132018-09-132009-02-10Proceedings of the National Academy of Sciences of the United States of America. Vol.106, No.6 (2009), 1790-179510916490002784242-s2.0-60549098792https://repository.li.mahidol.ac.th/handle/20.500.14594/28396Two 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. © 2009 by The National Academy of Sciences of the USA.Mahidol UniversityMultidisciplinaryArticleSCOPUS10.1073/pnas.0812752106