Publication Abstract from PubMed
Synthesis and detection of acyl-homoserine lactones (AHLs) enables many gram-negative bacteria to engage in quorum sensing, an intercellular signaling mechanism that activates differentiation to virulent and biofilm lifestyles. The AHL synthases catalyze acylation of S-adenosyl-L-methionine by acyl-acyl carrier protein and lactonization of the methionine moiety to give AHLs. The crystal structure of the AHL synthase, EsaI, determined at 1.8 A resolution, reveals a remarkable structural similarity to the N-acetyltransferases and defines a common phosphopantetheine binding fold as the catalytic core. Critical residues responsible for catalysis and acyl chain specificity have been identified from a modeled substrate complex and verified through functional analysis in vivo. A mechanism for the N-acylation of S-adenosyl-L-methionine by 3-oxo-hexanoyl-acyl carrier protein is proposed.
Structural basis and specificity of acyl-homoserine lactone signal production in bacterial quorum sensing.,Watson WT, Minogue TD, Val DL, von Bodman SB, Churchill ME Mol Cell. 2002 Mar;9(3):685-94. PMID:11931774[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
