Crystal structure at 1.2 Å resolution and active site mapping of Escherichia coli peptidyl‐tRNA hydrolase

@article{Schmitt1997CrystalSA,
  title={Crystal structure at 1.2 {\AA} resolution and active site mapping of Escherichia coli peptidyl‐tRNA hydrolase},
  author={E. Schmitt and Y. Mechulam and M. Fromant and P. Plateau and S. Blanquet},
  journal={The EMBO Journal},
  year={1997},
  volume={16}
}
Peptidyl‐tRNA hydrolase activity from Escherichia coli ensures the recycling of peptidyl‐tRNAs produced through abortion of translation. This activity, which is essential for cell viability, is carried out by a monomeric protein of 193 residues. The structure of crystalline peptidyl‐tRNA hydrolase could be solved at 1.2 Å resolution. It indicates a single α/β globular domain built around a twisted mixed β‐sheet, similar to the central core of an aminopeptidase from Aeromonas proteolytica. This… Expand
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