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: Structure, Function and Genetics

Volumn 71, Issue 2, 2008, Pages 1027-1031

  Singarapu, Kiran Kumar ^a,b   Xiao, Rong ^b,c   Acton, Thomas ^b,c   Rost, Burkhard ^b,d   Montelione, Gaetano T ^b,c   Szyperski, Thomas ^a,b  

^a UNIVERSITY AT BUFFALO   (United States)

^b Northeast Structural Genomics Consortium ^*

^c RUTGERS UNIVERSITY   (United States)

^d Och Spine at New York Presbyterian Hospitals   (United States)

Author keywords

GFT NMR; Peptidyl tRNA hydrolase domain; Protein translation; Release factors; Structural genomics

Indexed keywords

ENZYME; PEPTIDYL TRNA HYDROLASE; RELEASING FACTOR; RELEASING FACTOR 1; UNCLASSIFIED DRUG;

ARTICLE; HYDROLYSIS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE; PSEUDOMONAS SYRINGAE;

CARBOXYLIC ESTER HYDROLASES; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE TERMINATION FACTORS; PROTEIN STRUCTURE, TERTIARY; PSEUDOMONAS SYRINGAE;

PSEUDOMONAS SYRINGAE;

EID: 41149160381     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21947     Document Type: Article

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