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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
Author(s) -
Singarapu Kiran Kumar,
Xiao Rong,
Acton Thomas,
Rost Burkhard,
Montelione Gaetano T.,
Szyperski Thomas
Publication year - 2008
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.21947
Subject(s) - pseudomonas syringae , structural genomics , hydrolase , biochemistry , biology , peptide sequence , transfer rna , protein structure , chemistry , gene , rna , enzyme
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 Kiran Kumar Singarapu, Rong Xiao, Thomas Acton, Burkhard Rost, Gaetano T. Montelione, and Thomas Szyperski* 1Department of Chemistry, State University of New York at Buffalo, Buffalo, New York 14260-3000 2Northeast Structural Genomics Consortium 3Department of Molecular Biology and Biochemistry, Center of Advanced Biotechnology and Medicine, Rutgers University, Piscataway, New Jersey 08854-5638 4Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032

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