Functional guanine-arginine interaction between tRNAPro and prolyl-tRNA synthetase that couples binding and catalysis

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1784, Issue 9, 2008, Pages 1222-1225

  Burke, Brian ^a,c   An, Songon ^a,d   Musier Forsyth, Karin ^b  

^a University of Minnesota   (United States)

^b OHIO STATE UNIVERSITY   (United States)

^c Novartis Vaccines and Diagnostics   (United States)

^d PENNSYLVANIA STATE UNIVERSITY   (United States)

Author keywords

8 oxo guanosine; Aminoacyl tRNA synthetases; Coupling network; Oxidative cross linking; Prolyl tRNA synthetase; RNA protein interactions

Indexed keywords

AMINO ACID TRANSFER RNA LIGASE; ARGININE; GUANINE; HYDROGEN; TRANSFER RNA; BACTERIAL RNA; CROSS LINKING REAGENT; ESCHERICHIA COLI PROTEIN; PROLINE TRANSFER RNA; PROLYL T RNA SYNTHETASE; RECOMBINANT PROTEIN;

AMINOACYLATION; ANTICODON; ARTICLE; CHEMICAL INTERACTION; CROSS LINKING; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME PURIFICATION; ESCHERICHIA COLI; HYDROGEN BOND; PRIORITY JOURNAL; AMINO ACID SUBSTITUTION; CATALYSIS; CHEMISTRY; ENZYME SPECIFICITY; GENETICS; METABOLISM; OXIDATION REDUCTION REACTION; SITE DIRECTED MUTAGENESIS;

ESCHERICHIA COLI;

AMINO ACID SUBSTITUTION; AMINO ACYL-TRNA SYNTHETASES; ARGININE; CATALYSIS; CATALYTIC DOMAIN; CROSS-LINKING REAGENTS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GUANINE; HYDROGEN BONDING; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; RECOMBINANT PROTEINS; RNA, BACTERIAL; RNA, TRANSFER, PRO; SUBSTRATE SPECIFICITY;

EID: 53149085918     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.04.027     Document Type: Article

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