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首页> 外文期刊>Journal of Molecular Biology >Biosynthesis of isoprenoids: crystal structure of the (4Fe-4S) cluster protein IspG.
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Biosynthesis of isoprenoids: crystal structure of the (4Fe-4S) cluster protein IspG.

机译：类异戊二烯的生物合成：（4Fe-4S）簇蛋白IspG的晶体结构。

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摘要

IspG protein serves as the penultimate enzyme of the recently discovered non-mevalonate pathway for the biosynthesis of the universal isoprenoid precursors, isopentenyl diphosphate and dimethylallyl diphosphate. The enzyme catalyzes the reductive ring opening of 2C-methyl-D-erythritol 2,4-cyclodiphosphate, which affords 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. The protein was crystallized under anaerobic conditions, and its three-dimensional structure was determined to a resolution of 2.7 A. Each subunit of the c(2) symmetric homodimer folds into two domains connected by a short linker sequence. The N-terminal domain (N domain) is an eight-stranded beta barrel that belongs to the large TIM-barrel superfamily. The C-terminal domain (C domain) consists of a beta sheet that is flanked on both sides by helices. One glutamate and three cysteine residues of the C domain coordinate a [4Fe-4S] cluster. Homodimer formation involves an extended contact area (about 1100 A(2)) between helices 8 and 9 of each respective beta barrel. Moreover, each C domain contacts the N domain of the partner subunit, but the interface regions are small (about 430 A(2)). We propose that the enzyme substrate binds to the positively charged surface area at the C-terminal pole of the beta barrel. The C domain carrying the iron-sulfur cluster could then move over to form a closed conformation where the substrate is sandwiched between the N domain and the C domain. This article completes the set of three-dimensional structures of the non-mevalonate pathway enzymes, which are of specific interest as potential targets for tuberculostatic and antimalarial drugs.
机译：IspG蛋白是最近发现的非甲羟戊酸途径的倒数第二个酶，用于生物合成通用类异戊二烯前体，异戊烯基二磷酸和二甲基烯丙基二磷酸。该酶催化2C-甲基-D-赤藓糖醇2,4-环二磷酸的还原性开环，从而提供1-羟基-2-甲基-2-（E）-丁烯基4-二磷酸。该蛋白质在厌氧条件下结晶，其三维结构确定为2.7 A的分辨率。c（2）对称同型二聚体的每个亚基折叠成两个通过短接头序列连接的域。 N末端域（N域）是一个八链β桶，属于大TIM桶超家族。 C端结构域（C域）由一个β折叠组成，该折叠在两侧均带有螺旋。 C结构域的一个谷氨酸和三个半胱氨酸残基协调[4Fe-4S]簇。同质二聚体的形成涉及每个β桶各自的螺旋8和9之间的接触面积扩大（约1100 A（2））。此外，每个C结构域都接触伙伴亚基的N结构域，但界面区域很小（大约430 A（2））。我们建议酶底物结合到β桶的C末端极带正电的表面积。然后携带铁-硫簇的C结构域可以移动形成封闭的构象，其中底物夹在N结构域和C结构域之间。本文完成了非甲羟戊酸途径酶的三维结构，这是作为抗结核药和抗疟药的潜在靶标具有特殊意义的。

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