This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1k4j
From Proteopedia
|
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 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
Page seeded by OCA on Thu Feb 21 13:30:05 2008
