Structural basis and specificity of acyl-homoserine lactone signal production in bacterial quorum sensing

Mol Cell. 2002 Mar;9(3):685-94. doi: 10.1016/s1097-2765(02)00480-x.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • 4-Butyrolactone / analogs & derivatives
  • 4-Butyrolactone / biosynthesis*
  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Binding Sites
  • Gram-Negative Bacteria / enzymology*
  • Gram-Negative Bacteria / genetics
  • Models, Molecular
  • Molecular Sequence Data
  • Molecular Structure
  • Mutagenesis, Site-Directed
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Signal Transduction*
  • Substrate Specificity


  • Bacterial Proteins
  • EsaI protein, Erwinia stewartii
  • 4-Butyrolactone

Associated data

  • PDB/1K4J
  • PDB/1KZF