Crystallization and rhenium MAD phasing of the acyl-homoserinelactone synthase EsaI.
Crystallization and rhenium MAD phasing of the acyl-homoserinelactone synthase EsaI.
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酰基高丝氨酸内酯合酶 EsaI 的结晶和铼 MAD 定相。
DOI：
10.1107/s0907444901014512
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发表时间：
2001
期刊：
影响因子：
--
通讯作者：
Churchill,ME
中科院分区：
文献类型：
--
作者：
Watson,WT;Murphy4th,FV;Gould,TA;Jambeck,P;Val,DL;CronanJr,JE;BeckvonBodman,S;Churchill,ME
酰基高丝氨酸-L-内酯（AHL）是许多革兰氏阴性菌毒力所需的可扩散化学信号。AHL由阿勒脱氢酶从两种底物S-腺苷-L-甲硫氨酸和酰基-酰基载体蛋白产生。阿勒合酶Esa Ⅰ与其他病原菌的阿勒酶同源，属于原始四元空间群P43，晶胞参数a = B = 66.40，c = 47.33 nm。 该结构是通过多波长反常衍射与一种新的使用的非正常信号来解决。含铕的结构已被细化到2.5 μ m的分辨率，并已确定过氧化氢离子结合位点和配位残基。
Acyl-homoserine-l-lactones (AHLs) are diffusible chemical signals that are required for virulence of many Gram-negative bacteria. AHLs are produced by AHL synthases from two substrates, S-adenosyl-l-methionine and acyl-acyl carrier protein. The AHL synthase EsaI, which is homologous to the AHL synthases from other pathogenic bacterial species, has been crystallized in the primitive tetragonal space group P43, with unit-cell parameters a = b = 66.40, c = 47.33 Å. The structure was solved by multiple-wavelength anomalous diffraction with a novel use of the rhenium anomalous signal. The rhenium-containing structure has been refined to a resolution of 2.5 Å and the perrhenate ion binding sites and liganding residues have been identified.