Structure of fungal fatty acid synthase and implications for iterative substrate shuttling
Structure of fungal fatty acid synthase and implications for iterative substrate shuttling
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DOI：
10.1126/science.1138248
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发表时间：
2007-04-13
期刊：
影响因子：
56.9
通讯作者：
Ban, Nenad
中科院分区：
文献类型：
--
作者：
Jenni, Simon;Leibundgut, Marc;Ban, Nenad
我们报道了羊毛热霉菌2.6兆吨α(6)β(6)异十二聚体脂肪酸合成酶在3.1埃分辨率下的晶体结构。α和β多肽链形成脂肪酸合成所需的六个催化域和许多负责广泛亚基间连接的扩展片段。所有活性位点的详细视图提供了对底物特异性和催化机制的洞察，并揭示了它们的独特特征，这是由于整合到多酶中。酰基载体蛋白在反应室中的附着方式以及活性中心的空间分布表明，迭代底物穿梭是通过多功能酶中载体结构域相对受限的圆周运动实现的。
We report crystal structures of the 2.6-megadalton alpha(6)beta(6) heterododecameric fatty acid synthase from Thermomyces lanuginosus at 3.1 angstrom resolution. The alpha and beta polypeptide chains form the six catalytic domains required for fatty acid synthesis and numerous expansion segments responsible for extensive intersubunit connections. Detailed views of all active sites provide insights into substrate specificities and catalytic mechanisms and reveal their unique characteristics, which are due to the integration into the multienzyme. The mode of acyl carrier protein attachment in the reaction chamber, together with the spatial distribution of active sites, suggests that iterative substrate shuttling is achieved by a relatively restricted circular motion of the carrier domain in the multifunctional enzyme.