Crystal structures of the editing domain of Escherichia coli leucyl-tRNA synthetase and its complexes with Met and Ile reveal a lock-and-key mechanism for amino acid discrimination

Biochemical Journal

Volumn 394, Issue 2, 2006, Pages 399-407

  Liu, Yunqing ^a,b   Liao, Jing ^a,b   Zhu, Bin ^a,b   Wang, En Duo ^a   Ding, Jianping ^a  

^a INSTITUTE OF BIOCHEMISTRY AND CELL BIOLOGY   (China)

^b UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

Author keywords

Aminoacyl tRNA synthetase; Aminoacylation; Editing domain; Lock and key mechanism; Recognition

Indexed keywords

AMINO ACIDS; CRYSTAL STRUCTURE; ENZYME KINETICS; PROTEINS; RNA; SYNTHESIS (CHEMICAL);

AMINOACYLATION; EDITING DOMAIN; LOCK-AND-KEY MECHANISM; RECOGNITION;

ESCHERICHIA COLI;

AMINO ACID; ISOLEUCINE; LEUCINE; LEUCINE TRANSFER RNA LIGASE; METHIONINE; TRANSFER RNA;

AMINOACYLATION; ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; ESTERIFICATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; STEREOCHEMISTRY; STEREOSPECIFICITY; X RAY DIFFRACTION;

AMINO ACID SEQUENCE; BINDING SITES; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; ISOLEUCINE; LEUCINE-TRNA LIGASE; METHIONINE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

ESCHERICHIA COLI;

EID: 33644748247     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20051249     Document Type: Article

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