Structural basis and specificity of acyl-homoserine lactone signal production in bacterial quorum sensing
Structural basis and specificity of acyl-homoserine lactone signal production in bacterial quorum sensing
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DOI：
10.1016/s1097-2765(02)00480-x
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发表时间：
2002-03-01
期刊：
影响因子：
16
通讯作者：
Churchill, MEA
中科院分区：
文献类型：
--
作者：
Watson, WT;Minogue, TD;Churchill, MEA
酰基高丝氨酸内酯 (AHL) 的合成和检测使许多革兰氏阴性细菌能够参与群体感应，这是一种细胞间信号传导机制，可激活向有毒和生物膜生活方式的分化。 AHL合酶催化酰基-酰基载体蛋白对S-腺苷-L-甲硫氨酸的酰化以及甲硫氨酸部分的内酯化以产生AHL。 AHL 合酶 Esal 的晶体结构以 1.8 埃分辨率测定，揭示了与 N-乙酰转移酶显着的结构相似性，并将常见的磷酸泛硫氨酸结合折叠定义为催化核心。负责催化和酰基链特异性的关键残基已从模拟底物复合物中鉴定出来，并通过体内功能分析进行验证。提出了 3-氧代己酰基-酰基载体蛋白对 S-腺苷-L-甲硫氨酸进行 N-酰化的机制。
Synthesis and detection of acyll-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, Esal, determined at 1.8 Angstrom 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-oxohexanoyl-acyl carrier protein is proposed.