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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...
Tallennettuna:
| Päätekijät: | , , , , , |
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| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
National Academy of Sciences
2009
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| 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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