Three-dimensional structure of the quorum-quenching N-acyl homoserine lactone hydrolase from Bacillus thuringiensis

Proceedings of the National Academy of Sciences of the United States of America

Volumn 102, Issue 33, 2005, Pages 11882-11887

  Liu, Dali ^b   Lepore, Bryan W ^b   Petsko, Gregory A ^b   Thomas, Pei W ^a   Stone, Everett M ^a   Fast, Walter ^a   Ringe, Dagmar ^b  

^a UNIVERSITY OF TEXAS AT AUSTIN   (United States)

^b BRANDEIS UNIVERSITY   (United States)

Author keywords

Bridged bimetallo center; Lactonase; Single wavelength anomalous dispersion

Indexed keywords

BETA LACTAMASE; CARBOXYLIC ACID; GLUCONOLACTONASE; HYDROLASE; HYDROXIDE; LACTONE; METALLO BETA LACTAMASE; N ACYL HOMOSERINE LACTONE HYDROLASE; N ACYL HOMOSERINE LACTONE HYDROLASE LACTONASE; UNCLASSIFIED DRUG; ZINC ION;

ARTICLE; BACILLUS THURINGIENSIS; CELL DENSITY; ENZYME ACTIVE SITE; ENZYME DEGRADATION; ENZYME STRUCTURE; GRAM NEGATIVE BACTERIUM; HYDROLYSIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PATHOGENICITY; PRIORITY JOURNAL; SIGNAL TRANSDUCTION; THREE DIMENSIONAL IMAGING;

BACILLUS THURINGIENSIS; BINDING SITES; CARBOXYLIC ESTER HYDROLASES; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; GLYCEROL; MODELS, BIOLOGICAL; MODELS, MOLECULAR; PROTEIN STRUCTURE, TERTIARY; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; ZINC;

BACILLUS THURINGIENSIS; NEGIBACTERIA;

EID: 23844552796     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0505255102     Document Type: Article

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