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首页> 外文期刊>Molecular cell >Structural Basis and Specificity of Acyl-Homoserine Lactone Signal Production in Bacterial Quorum Sensing
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Structural Basis and Specificity of Acyl-Homoserine Lactone Signal Production in Bacterial Quorum Sensing

机译：细菌群体感应中酰基-高丝氨酸内酯信号产生的结构基础和特异性

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摘要

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, Esal, 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.
机译：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，群体感应是一种机制，可激活分化为有毒和生物膜的生活方式。 AHL合成酶通过酰基-酰基载体蛋白催化S-腺苷-L-蛋氨酸的酰化和蛋氨酸部分的内酯化以生成AHL。 AHL合酶Esal的晶体结构以1.8 A的分辨率测定，显示出与N-乙酰基转移酶显着的结构相似性，并定义了一个常见的磷酸泛肽结合折叠作为催化核心。已从建模的底物复合物中鉴定出负责催化和酰基链特异性的关键残基，并通过体内功能分析进行了验证。提出了3-氧代己酰基酰基载体蛋白对S-腺苷-L-蛋氨酸进行N-酰化的机理。

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