Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 1. Product-bound structures

Biochemistry

Volumn 47, Issue 29, 2008, Pages 7706-7714

  Liu, Dali ^a   Momb, Jessica ^b   Thomas, Pei W ^b   Moulin, Aaron ^a   Petsko, Gregory A ^a   Fast, Walter ^b   Ringe, Dagmar ^a  

^a BRANDEIS UNIVERSITY   (United States)

^b UNIVERSITY OF TEXAS AT AUSTIN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOLOGY; COORDINATION REACTIONS; ENZYMES; FOOD ADDITIVES; MECHANISMS; METALS; QUANTUM CHEMISTRY; QUENCHING; THREE DIMENSIONAL; ZINC; ZINC SULFIDE;

AMERICAN CHEMICAL SOCIETY (ACS); BACILLUS THURINGIENSIS (BT); CATALYTIC MECHANISMS; DINUCLEAR; HOMOCYSTEINE (HCY); HOMOSERINE; HOMOSERINE LACTONES; HYDROLASES; LACTAMASE; LACTONASE; METAL CO-ORDINATION; METALLOENZYME; PRODUCT CONFIGURATIONS; PROTEIN CONFORMATIONS; QUORUM SENSING (QS); RING-OPENING; SUBSTRATE BINDING (SBD); THREE-DIMENSIONAL (3D) STRUCTURING;

MODEL STRUCTURES;

GLUCONOLACTONASE; HYDROLASE; METALLO BETA LACTAMASE; N ACYLHOMOSERINE LACTONE; N HEXANOYLHOMOSERINE LACTONE; THIOLACTONE; ZINC;

ARTICLE; BACILLUS THURINGIENSIS; COMPLEX FORMATION; CRYSTALLIZATION; ENZYME ACTIVE SITE; ENZYME STABILITY; ENZYME STRUCTURE; HYDROLYSIS; NONHUMAN; OPTICAL RESOLUTION; PHENOTYPE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; QUORUM SENSING; RING OPENING; THREE DIMENSIONAL IMAGING;

BACILLUS THURINGIENSIS; BACTERIAL PROTEINS; BINDING SITES; CARBOXYLIC ESTER HYDROLASES; CRYSTALLOGRAPHY, X-RAY; MODELS, MOLECULAR; MOLECULAR STRUCTURE; QUORUM SENSING;

BACILLUS THURINGIENSIS; BACTERIA (MICROORGANISMS);

EID: 47649131677     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi800368y     Document Type: Article

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