NMR structure of the peptidyl-tRNA hydrolase domain from Pseudomonas syringae expands the structural coverage of the hydrolysis domains of class 1 peptide chain release factors

Proteins. 2008 May 1;71(2):1027-31. doi: 10.1002/prot.21947.

Abstract

The NMR structure of the peptidyl-tRNA hydrolase (PTH) domain from Pseudomonas syringae (P. syringae PTH domain) was solved by using recently devised protocol for high throughput protein structure determination. The P. syringae PTH domain belongs to a large Pfam family PF00472, which consists of at least 1549 proteins annotated as ‘hydrolysis domains of peptidyl-tRNA’. The structure of P. syringae PTH domain expands the ‘structural coverage’ of the PFam family.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Carboxylic Ester Hydrolases / chemistry*
  • Models, Molecular
  • Nuclear Magnetic Resonance, Biomolecular
  • Peptide Termination Factors / chemistry*
  • Protein Structure, Tertiary
  • Pseudomonas syringae / enzymology

Substances

  • Peptide Termination Factors
  • Carboxylic Ester Hydrolases
  • aminoacyl-tRNA hydrolase