一个Fe2+结合缺陷的仿真病毒原 lysyl氧化酶的结构
Tingfei Chen1, Christoph Buhlheller2, Houfu Guo1
1Department of Molecular and Cellular Biochemistry, Markey Cancer Center, University of Kentucky, 741 South Limestone Avenue, Lexington, KY 40536-0509, USA.
概括
原 lysyl 氧化酶对原体结构至关重要. 这项研究表明,一个特定的铁结合点,而不是另一个,稳定了这些酶,澄清了它们的二分化机制.
科学领域:
- 生物化学 生物化学
- 结构生物学 结构生物学
- 酶学 是一种酶学.
背景情况:
- 原 lysyl氧酶 (LH) 是动物和仿真病毒中重要的酶,催化素氧化,用于原纤维化和功能.
- 以前的研究表明,LH对Fe2+的亲和力很高,Fe2+结合稳定酶二次体,但机制仍然难以捉摸.
- 结构分析揭示了仿真病毒LH中的Fe2+协调的2His-1Asp三合体,潜在的替代三合体表明双Fe2+结合点.
研究的目的:
- 为了研究仿真病毒LH中的替代2His-1Asp三元是否结合Fe2+.
- 阐明Fe2+结合调节LH二分化过程的机制.
- 确定LH二次体的Fe2+介导稳定性的结构基础.
主要方法:
- 一种仿真病毒酸酶突变体 (His825Ala) 的结晶,缺少一个2His-1Asp三合体.
- 在Fe2+的存在下分析His825Ala突变体的结构的X射线晶体学.
- 野生类型和突变酶之间的比较结构分析,以确定构造变化.
主要成果:
- 在His825Ala突变中的替代2His-1Asp三元组没有结合Fe2+,表明它对金属没有很高的亲和力.
- 结合Fe2+不涉及替代三合体,这表明主要的2His-1Asp三合体负责Fe2+的协调.
- His825Ala突变体形成的二元体类似于野生类型的酶,但在临界二元化残留物附近的形状变化,如Leu873.
结论:
- 替代的2His-1Asp三元组不是仿真病毒lysyl氧酶中的高亲和度Fe2+结合位.
- 结合Fe2+和随后的LH二分化调节涉及主要2His-1Asp三合体内的特定残留物.
- 对Fe2+结合和二元化的结构洞察力为了解原基氧酶的功能和调节提供了基础.
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