Crystallization and X-ray diffraction studies of a complete bacterial fatty-acid synthase type I
Crystallization and X-ray diffraction studies of a complete bacterial fatty-acid synthase type I
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DOI：
10.1107/s2053230x15018336
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发表时间：
2015-11-01
影响因子：
0.9
通讯作者：
Grininger, Martin
中科院分区：
文献类型：
--
作者：
Enderle, Mathias;McCarthy, Andrew;Grininger, Martin
虽然近年来对真菌和哺乳动物多酶I型脂肪酸合成酶（FAS I）有了深入的了解，但对狭窄分布于放线菌属分支杆菌、棒状杆菌和诺卡菌属的细菌FAS I家族仍知之甚少。这是特别相关的两个原因：(i)虽然与真菌FAS i同源，但低温电镜研究表明细菌FAS i具有独特的结构和功能特性；（ii）结核分枝杆菌FAS i是治疗结核病（TB）的药物靶点，因此作为药物靶点非常重要。产自C. efficiens的FAS I晶体，它是结核分枝杆菌FAS I的同源物，用x射线衍射到4.5埃的分辨率。
While a deep understanding of the fungal and mammalian multi-enzyme type I fatty-acid synthases (FAS I) has been achieved in recent years, the bacterial FAS I family, which is narrowly distributed within the Actinomycetales genera Mycobacterium, Corynebacterium and Nocardia, is still poorly understood. This is of particular relevance for two reasons: (i) although homologous to fungal FAS I, cryo-electron microscopic studies have shown that bacterial FAS I has unique structural and functional properties, and (ii) M. tuberculosis FAS I is a drug target for the therapeutic treatment of tuberculosis (TB) and therefore is of extraordinary importance as a drug target. Crystals of FAS I from C. efficiens, a homologue of M. tuberculosis FAS I, were produced and diffracted X-rays to about 4.5 angstrom resolution.