Structure-function studies of Escherichia coliRnlA reveal a novel toxin structure involved in bacteriophage resistance

Molecular Microbiology

Volumn 90, Issue 5, 2013, Pages 956-965

  Wei, Yong ^a,b   Gao, Zeng Qiang ^b   Otsuka, Yuichi ^c   Naka, Kenta ^c   Yonesaki, Tetsuro ^c   Zhang, Heng ^b   Dong, Yu Hui ^b  

^a UNIVERSITY OF SCIENCE AND TECHNOLOGY OF CHINA   (China)

^b INSTITUTE OF HIGH ENERGY PHYSICS   (China)

^c OSAKA UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL TOXIN; MONOMER; RNLA TOXIN; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL VIRULENCE; BACTERIOPHAGE; CARBOXY TERMINAL SEQUENCE; CELLULAR DISTRIBUTION; CHEMICAL INTERACTION; CRYSTAL STRUCTURE; DIMERIZATION; ESCHERICHIA COLI; IN VITRO STUDY; IN VIVO STUDY; INHIBITION KINETICS; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; STRUCTURE ACTIVITY RELATION; TOXIN STRUCTURE; X RAY CRYSTALLOGRAPHY;

ESCHERICHIA;

BACTERIAL TOXINS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI K12; ESCHERICHIA COLI PROTEINS; GENE EXPRESSION REGULATION, BACTERIAL; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SCATTERING, SMALL ANGLE; SEQUENCE HOMOLOGY, AMINO ACID; VIRAL PROTEINS;

EID: 84888311378     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12409     Document Type: Article

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