The CP2 domain of leucyl-tRNA synthetase is crucial for amino acid activation and post-transfer editing

Journal of Biological Chemistry

Volumn 283, Issue 52, 2008, Pages 36608-36616

  Zhou, Xiao Long ^a   Zhu, Bin ^a   Wang, En Duo ^a,b  

^a INSTITUTE OF BIOCHEMISTRY AND CELL BIOLOGY   (China)

^b NONE   (China)

Author keywords

[No Author keywords available]

Indexed keywords

AMINATION; AMINO ACIDS; BINDING ENERGY; ESCHERICHIA COLI; ORGANIC ACIDS;

ACID ACTIVATIONS; BINDING AFFINITIES; GIARDIA LAMBLIA; GLOBAL STRUCTURES; PRIMARY SEQUENCES; PYROCOCCUS HORIKOSHII; SITE-DIRECTED MUTAGENESIS; SYNTHETASE;

AMINES;

ALANINE; CONNECTIVE PEPTIDE 2; LEUCINE; LEUCINE TRANSFER RNA LIGASE; PEPTIDE; UNCLASSIFIED DRUG;

AMINOACYLATION; ARTICLE; BINDING AFFINITY; ESCHERICHIA COLI; GIARDIA LAMBLIA; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN FUNCTION; PYROCOCCUS HORIKOSHII; SITE DIRECTED MUTAGENESIS;

ALANINE; AMINO ACID SEQUENCE; ANIMALS; ESCHERICHIA COLI; GIARDIA LAMBLIA; HYDROLYSIS; LEUCINE; LEUCINE-TRNA LIGASE; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN STRUCTURE, TERTIARY; PYROCOCCUS HORIKOSHII; RNA EDITING; RNA, TRANSFER; SEQUENCE HOMOLOGY, AMINO ACID;

ESCHERICHIA COLI; GIARDIA INTESTINALIS; PROKARYOTA; PYROCOCCUS HORIKOSHII;

EID: 61349117470     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M806745200     Document Type: Article

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