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

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 cluste...

Täydet tiedot

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Bibliografiset tiedot
Päätekijät: Laowanapiban, Poramaet, Kapustina, Maryna, Vonrhein, Clemens, Delarue, Marc, Koehl, Patrice, Carter, Charles W.
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: National Academy of Sciences 2009
Aiheet:
Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC2644116/
https://ncbi.nlm.nih.gov/pubmed/19174517
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0812752106
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