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首页> 外文期刊>Journal of Molecular Biology >Crystal structures of Enoyl-ACP reductases I (FabI) and III (FabL) from B. subtilis.
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Crystal structures of Enoyl-ACP reductases I (FabI) and III (FabL) from B. subtilis.

机译：枯草芽孢杆菌Enoyl-ACP还原酶I（FabI）和III（FabL）的晶体结构。

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摘要

Enoyl-[acyl carrier protein] (ACP) reductase (ENR) is a key enzyme in type II fatty acid synthesis that catalyzes the last step in each elongation cycle. Therefore, it has been considered as a target for antibiotics. However, recent studies indicate that some pathogens have more than one ENR; in particular, Bacillus subtilis has two ENRs, FabI and FabL. The crystal structures of the ternary complexes of BsFaBI and BsFabL are found as a homotetramer showing the same overall structure despite a sequence identity of only 24%. The positions of the catalytic dyad of Tyr-(Xaa)(6)-Lys in FabL are almost identical to that of FabI, but a detailed structural analysis shows that FabL shares more structural similarities with FabG and other members of the SDR (short-chain alcohol dehydrogenase/reductase) family. The apo FabL structure shows significantly different conformations at the cofactor and the substrate-binding regions, and this resulted in a totally different tetrameric arrangement reflecting the flexibility of these regions in the absence of the cofactor and substrate/inhibitor.
机译：烯酰基-[酰基载体蛋白]（ACP）还原酶（ENR）是II型脂肪酸合成中的关键酶，可催化每个延长周期的最后一步。因此，它被认为是抗生素的靶标。但是，最近的研究表明，某些病原体具有不止一种的ENR。特别地，枯草芽孢杆菌具有两个ENR，FabI和FabL。发现BsFaBI和BsFabL的三元复合物的晶体结构是同源四聚体，尽管序列同一性仅为24％，但显示出相同的总体结构。 Tyr-（Xaa）（6）-Lys催化二元组在FabL中的位置几乎与FabI相同，但详细的结构分析表明FabL与FabG和SDR的其他成员具有更多的结构相似性（链醇脱氢酶/还原酶）家族。载脂蛋白FabL结构在辅因子和底物结合区域显示出显着不同的构象，这导致完全不同的四聚体排列，反映出在没有辅因子和底物/抑制剂的情况下这些区域的柔性。

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