3DHA

An Ultral High Resolution Structure of N-Acyl Homoserine Lactone Hydrolase with the Product N-Hexanoyl-L-Homoserine Bound at An Alternative Site

Summary for 3DHA

• Entry DOI: 10.2210/pdb3dha/pdb
• Related: 2A7M 2R2D 3DHB 3DHC
• Descriptor: N-Acyl Homoserine Lactone Hydrolase, ZINC ION, N-hexanoyl-L-homoserine, ... (5 entities in total)
• Functional Keywords: zinc bimetallohydrolase, quorum quenching, n-acyl homoserine lactone, alternative binding site, product complex, ahl lactonase, hydrolase
• Biological source: Bacillus thuringiensis serovar kurstaki
• Total number of polymer chains: 1
• Total formula weight: 29381.10

Authors

Liu, D.,Momb, J.,Thomas, P.W.,Moulin, A.,Petsko, G.A.,Fast, W.,Ringe, D. (deposition date: 2008-06-17, release date: 2008-07-29, Last modification date: 2023-08-30)

• Primary citation: Liu, D.,Momb, J.,Thomas, P.W.,Moulin, A.,Petsko, G.A.,Fast, W.,Ringe, D.; Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 1. Product-bound structures.; Biochemistry, 47:7706-7714, 2008; PubMed: 18627129; DOI: 10.1021/bi800368y

Experimental method

X-RAY DIFFRACTION (0.95 Å)