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1K4J

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

Summary for 1K4J
Entry DOI10.2210/pdb1k4j/pdb
Related1kzf
Descriptoracyl-homoserinelactone synthase EsaI, PERRHENATE (3 entities in total)
Functional Keywordsacyl-homoserinelactone synthase, mixed alpha beta, enzyme, gnat similarity, quorum sensing, autoinducer synthase, ligase
Biological sourcePantoea stewartii subsp. stewartii
Total number of polymer chains1
Total formula weight27792.16
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 citationWatson, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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数据于2024-10-30公开中

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