Molecular basis for the substrate specificity of quorum signal synthases

Abstract

Significance These first structures of a homoserine-lactone quorum-signal synthase bound to various substrates and analogs help to provide a molecular rationale for understanding acyl chain specificity. Based on the structural data, we show how different clades of signal synthases can accommodate their cognate acyl–CoA ligands. Lastly, the elucidation of the reaction mechanism for the signal synthase may provide a rationale for the design of therapeutic small-molecule antagonists.