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Article

Crystal structure at 1.2 A resolution and active site mapping of Escherichia coli peptidyl-tRNA hydrolase.

The EMBO journal - 1 Aug 1997

Schmitt E, Mechulam Y, Fromant M, Plateau P, Blanquet S

Abstract excerpt

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 A resolution. It indicates a single alpha/beta globular domain built around a twisted mixed...

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Identifiers

PMID: 9303320
DOI: 10.1093/emboj/16.15.4760
PMCID: PMC1170102

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