1k4j

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

spinqualitylabelsall models 1k4j, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1k4j is a 1 chain structure with sequence from Pantoea stewartii subsp. stewartii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: REO Related: 1kzf Gene: esaI/esaR cluster (Pantoea stewartii subsp. stewartii) Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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