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菌根菌的ergothioneine-biosynthesis C-S溶酶 EgtE 的结构

Lili Wei¹, Lei Liu¹, Weimin Gong¹

¹School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, China.

The Journal of biological chemistry

|December 10, 2023

概括

这项研究揭示了第一种来自Mycobacterium smegmatis的ergothioneine生物合成C-S溶酶 (EgtE) 的细菌结构. 它强调了与真菌酶相比的主要活性部位残留物和基质识别的差异,表明了趋同的进化.

科学领域:

生物化学生物化学
结构生物学结构生物学
微生物学微生物学

背景情况:

L-ergothioneine 是微生物产生的重要化合物,影响其生理学和病原性.
欧戈氨酸的生物合成涉及一种依赖于酸盐的C-S溶酶,这对于L-欧戈氨酸的生产至关重要.
了解这些酶是解读微生物代谢途径和相互作用的关键.

研究的目的:

为了确定Mycobacterium smegmatis ergothioneine-biosynthesis C-S lyase (MsEgtE) 的晶体结构.
分析活性部位残留物及其在酶反应中的作用.
为了比较细菌和真菌的C-S酶,了解基质识别和进化分歧.

主要方法:

采用X射线结晶学来获得MsEgtE.的3D结构.
在MsEgtE和真菌同源NcEgt2.2之间进行了序列和结构比较.
分析的重点是活性部位残留物和参与基质结合的保存基因.

主要成果:

确定了第一个ergothioneine生物合成C-S溶酶MsEgtE的细菌结构.
MsEgtE与真菌Egt2具有结构上的相似性,但表现出不同的基底识别机制.
保存的氨酸残留物 (Arg348) 对于物种间的基质识别至关重要,在细菌EgtE.中存在独特的α-螺旋 (α14).

结论:

对 MsEgtE 的结构洞察力为了解细菌的欧戈氨酸生物合成提供了基础.
细菌和真菌酶之间的基质识别差异突显了进化适应.
细菌EgtE中独特的α14螺旋体表明L-ergothioneine的生物合成中的融合进化.

关键词:

这位女士是什么意思? MsEgtE 这是Mycobacterium.没有了,没有了,没有了.埃尔戈氨酸生物合成C-S溶酶蛋白质结构蛋白质结构氧化还原稳定性恒常性 (ergothioneine) 是一种

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