构成性内皮氧化合成酶的晶体结构:涉及新型金属中心的蛋白功能的一个范例
1Department of Molecular Biology and Biochemistry, University of California, Irvine 92697-3900, USA.
Cell
|January 6, 1999
概括
研究人员确定了内皮氧化合成酶 (NOS) 的晶体结构,揭示了离子.
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:
- 氧化 (NO) 是一种由氧化合成酶 (NOS) 合成的关键信号分子.
- 内皮NOS (eNOS) 在心血管功能中起着至关重要的作用.
- 了解eNOS结构是阐明其催化机制的关键.
研究的目的:
- 为了确定内皮NOS血红质域的晶体结构.
- 调查离子和四生物 (H4B) 结合部位的结构作用.
- 为eNOS催化循环提出一个模型.
主要方法:
- 使用X射线晶体学来获得高分辨率的结构.
- 确定了eNOS血红域的四二二素 (H4B) 无和结合形式的结构.
- 分析蛋白质 - 配体相互作用和金属协调.
主要成果:
- 在1.95 Å (无H4B) 和1.9 Å (有H4B) 时,eNOS血红域的晶体结构得到了解决.
- 一个离子在二元界面上的类残留物以四面体协调,稳定了H4B结合部位.
- 意外地在H4B部位发现了L-氨酸,这表明它在稳定阴离子原体中的作用.
结论:
- 中心对于保持eNOS中的H4B结合位点的结构完整性至关重要.
- H4B部位容纳了L-氨酸,这表明了一个新的基质结合机制.
- 提出了一种涉及eNOS催化循环中的阴离子基的模型.
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