4J5H

Crystal Structure of B. thuringiensis AiiA mutant F107W with N-decanoyl-L-homoserine bound at the active site

Summary for 4J5H

• Entry DOI: 10.2210/pdb4j5h/pdb
• Related: 4J5F
• Descriptor: N-acyl homoserine lactonase, ZINC ION, N-decanoyl-L-homoserine, ... (5 entities in total)
• Functional Keywords: aiia, lactonase, dizinc hydrolase, substrate specificity, quorum quenching, beta-hairpin loops, n-acyl homoserine lactone, hydrolase-hydrolase substrate complex, hydrolase/hydrolase substrate
• Biological source: Bacillus thuringiensis
• Total number of polymer chains: 1
• Total formula weight: 29844.62

Authors

Liu, C.F.,Liu, D.,Momb, J.,Thomas, P.W.,Lajoie, A.,Petsko, G.A.,Fast, W.,Ringe, D. (deposition date: 2013-02-08, release date: 2013-06-26, Last modification date: 2024-02-28)

• Primary citation: Liu, C.F.,Liu, D.,Momb, J.,Thomas, P.W.,Lajoie, A.,Petsko, G.A.,Fast, W.,Ringe, D.; A phenylalanine clamp controls substrate specificity in the quorum-quenching metallo-gamma-lactonase from Bacillus thuringiensis.; Biochemistry, 52:1603-1610, 2013; PubMed: 23387521; DOI: 10.1021/bi400050j

Experimental method

X-RAY DIFFRACTION (1.45 Å)