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1k4j
From Proteopedia
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Crystal Structure of the Acyl-homoserinelactone Synthase EsaI Complexed with Rhenate
Overview
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.
About this Structure
1K4J is a Single protein structure of sequence from Pantoea stewartii subsp. stewartii with REO as ligand. Full crystallographic information is available from OCA.
Reference
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
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