1K4J

Crystal Structure of the Acyl-homoserinelactone Synthase EsaI Complexed with Rhenate

Summary for 1K4J

• Entry DOI: 10.2210/pdb1k4j/pdb
• Related: 1kzf
• Descriptor: acyl-homoserinelactone synthase EsaI, PERRHENATE (3 entities in total)
• Functional Keywords: acyl-homoserinelactone synthase, mixed alpha beta, enzyme, gnat similarity, quorum sensing, autoinducer synthase, ligase
• Biological source: Pantoea stewartii subsp. stewartii
• Total number of polymer chains: 1
• Total formula weight: 27792.16

Authors

Watson, W.T.,Minogue, T.D.,Val, D.L.,Beck von Bodman, S.,Churchill, M.E.A. (deposition date: 2001-10-08, release date: 2002-04-17, Last modification date: 2024-02-07)

Primary citation

Watson, W.T.,Minogue, T.D.,Val, D.L.,von Bodman, S.B.,Churchill, M.E.
Structural basis and specificity of acyl-homoserine lactone signal production in bacterial quorum sensing.
Mol.Cell, 9:685-694, 2002

PubMed Abstract: 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.

PubMed: 11931774
DOI: 10.1016/S1097-2765(02)00480-X

Experimental method

X-RAY DIFFRACTION (2.5 Å)