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TitleNMR 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.
Journal, issue, pagesProteins, Vol. 71, Page 1027-1031, Year 2008
Publish dateSep 14, 2007 (structure data deposition date)
AuthorsSingarapu, K.K. / Xiao, R. / Acton, T. / Rost, B. / Montelione, G.T. / Szyperski, T.
External linksProteins / PubMed:18247350
MethodsNMR (solution)
Structure data

PDB-2jva:
NMR solution structure of peptidyl-tRNA hydrolase domain protein from Pseudomonas syringae pv. tomato. Northeast Structural Genomics Consortium target PsR211
Method: SOLUTION NMR

Source
  • pseudomonas syringae pv. tomato (bacteria)
KeywordsHYDROLASE / GFT NMR / Structural Genomics / PSI-2 / Protein Structure Initiative / Northeast Structural Genomics Consortium / NESG

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