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© Structural Dynamics Of Macromolecules
The structure of a bacterial analog of the nicotinic receptor (one color per subunit) inserted into the cell membrane (grey and orange). A representation of the volume accessible to ions is shown in yellow.
Publication : Proceedings of the National Academy of Sciences of the United States of America

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

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Proceedings of the National Academy of Sciences of the United States of America - 27 Jan 2009

Laowanapiban P, Kapustina M, Vonrhein C, Delarue M, Koehl P, Carter CW

Link to Pubmed [PMID] – 19174517

Proc. Natl. Acad. Sci. U.S.A. 2009 Feb;106(6):1790-5

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://www.ncbi.nlm.nih.gov/pubmed/19174517