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首页> 外文期刊>Journal of Molecular Biology >Atomic Resolution Structure of a Succinimide Intermediate in E.coli CheY.
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Atomic Resolution Structure of a Succinimide Intermediate in E.coli CheY.

机译：大肠杆菌CheY中琥珀酰亚胺中间体的原子拆分结构。

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摘要

Isomerization of aspartate to isoaspartate occurs spontaneously in proteins, causes changes in protein structures, and correlates positively with the aging processes of many organisms, including Alzheimer disease in humans. Aspartate isomerization proceeds through an unstable cyclic succinimide intermediate. There are few protein structure determinations that have characterized the intermediates and products of this isomerization reaction. Here we report the discovery of an unusually stabilized succinimide ring in the 1.1A structure of the Escherichia coli CheY protein, as determined from a crystal eight years old. The ring is formed by the side-chain of aspartate 75 and the backbone nitrogen of glycine 76 in an exposed loop of the molecule. Stabilization of the succinimide is through interaction of a sulfate ion oxygen atom with the imide nitrogen atom. Formation of the ring caused conformational changes in the loop, but did not alter the overall structure of the protein.
机译：天冬氨酸异构化为异天冬氨酸在蛋白质中自发发生，引起蛋白质结构变化，并与许多生物的衰老过程呈正相关，包括人类的阿尔茨海默氏病。天冬氨酸异构化通过不稳定的环状琥珀酰亚胺中间体进行。很少有蛋白质结构测定可以表征这种异构化反应的中间体和产物。在这里，我们报道了从八岁的晶体中发现的，在大肠杆菌CheY蛋白的1.1A结构中发现异常稳定的琥珀酰亚胺环的发现。该环由天冬氨酸75的侧链和甘氨酸76的主链氮在分子的暴露环中形成。琥珀酰亚胺的稳定化是通过硫酸根离子氧原子与酰亚胺氮原子的相互作用来实现的。环的形成引起环中的构象变化，但没有改变蛋白质的整体结构。

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