Recognition of Intermediate Functionality by Acyl Carrier Protein over a Complete Cycle of Fatty Acid Biosynthesis
Recognition of Intermediate Functionality by Acyl Carrier Protein over a Complete Cycle of Fatty Acid Biosynthesis
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DOI：
10.1016/j.chembiol.2010.05.024
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发表时间：
2010-07-30
影响因子：
--
通讯作者：
Crump, Matthew P.
中科院分区：
文献类型：
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作者：
Ploskon, Eliza;Arthur, Christopher J.;Crump, Matthew P.
目前尚不清楚在细菌脂肪酸合成酶（FAS）中酰基链转移是程序化的还是扩散控制的和随机的。酰基载体蛋白（ACP）传递所有中间体并与所有合酶相互作用，在这一过程中起着关键作用。共价结合ACP的中间体的高分辨率结构代表脂肪酸生物合成的每一步已经解决了溶液核磁共振。这些化合物包括来自冷色链霉菌FAS的己醇基-、3-氧辛烷基-、3r -羟基辛烷基-、2-辛烷基-和辛烷酰acp。高分辨率结构揭示了ACP在内部脂肪酸结合口袋变化的驱动下对每个中间体采用独特的构象。每个中间体的结合显示出保守的结构特征，可以确保在随后的脂肪酸生物合成过程中有效的分子识别。
It remains unclear whether in a bacterial fatty acid synthase (FAS) acyl chain transfer is a programmed or diffusion controlled and random action. Acyl carrier protein (ACP), which delivers all intermediates and interacts with all synthase enzymes, is the key player in this process. High-resolution structures of intermediates covalently bound to an ACP representing each step in fatty acid biosynthesis have been solved by solution NMR. These include hexanoyl-, 3-oxooctanyl-, 3R-hydroxyoctanoyl-, 2-octenoyl-, and octanoyl-ACP from Streptomyces coelicolor FAS. The high-resolution structures reveal that the ACP adopts a unique conformation for each intermediate driven by changes in the internal fatty acid binding pocket. The binding of each intermediate shows conserved structural features that may ensure effective molecular recognition over subsequent rounds of fatty acid biosynthesis.