Independent saturation of three TrpRS subsites generates a partially assembled state similar to those observed in molecular simulations.
Proc Natl Acad Sci U S A
; 106(6): 1790-5, 2009 Feb 10.
Article
em En
| MEDLINE
| ID: mdl-19174517
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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1
Base de dados:
MEDLINE
Assunto principal:
Geobacillus stearothermophilus
/
Triptofano-tRNA Ligase
Idioma:
En
Ano de publicação:
2009
Tipo de documento:
Article