Atomic resolution structure of a succinimide intermediate in E.coli CheY.

Atomic resolution structure of a succinimide intermediate in E.coli CheY.
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大肠杆菌 CheY 中琥珀酰亚胺中间体的原子分辨率结构。

DOI:
10.1016/s0022-2836(02)00821-5
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发表时间:
2002
影响因子:
5.6
通讯作者:
Volz,Karl
Volz,Karl
中科院分区:
生物学2区
文献类型:
--
作者:
Simonovic,Miljan;Volz,Karl

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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 1.1Å 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.
野生型 ApoCheY* 1.1-Å 分辨率结构中独特的元活性构象
DOI: --
发表时间: 2001
影响因子: 4.8
作者:
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