人类细胞视网膜甲结合蛋白具有二次热9-cis-视网膜异构酶活性
Christin S Bolze1, Rachel E Helbling, Robin L Owen
1Department of Chemistry and Biochemistry, and ‡Graduate School for Cellular and Biomedical Sciences, University of Bern , Freiestrasse 3, 3012 Bern, Switzerland.
Journal of the American Chemical Society
|December 17, 2013
概括
细胞视网膜脱结合蛋白 (CRALBP) 表现出二次异构酶活性,将9-cis-retinal转化为9,13-dicis-retinal. 这个过程是由蛋白质内的水分子网络促进的.
科学领域:
- 生物化学 生物化学
- 分子生物学分子生物学
- 结构生物学 结构生物学
背景情况:
- 细胞视网膜甲结合蛋白 (CRALBP) 对于视觉色素再生至关重要.
- CRALBP通常是11-cis-retinal的陪伴者,用于素相互作用.
研究的目的:
- 为了研究CRALBP的二次异构酶活性.
- 为了阐明CRALBP催化9-cis-retinal的异构化机制.
主要方法:
- 紫外线/紫外线光谱学和 (1) H NMR光谱学用于产品特征.
- 一个与9-cis-retinal.complexed的CRALBP突变体的X射线晶体学.
- 计算分析,动力学研究和位点定向突变发生.
主要成果:
- CRALBP 显示在 9-cis-视网膜上具有热异构酶活性,产生 9,13-dicis-视网膜.
- 与11-cis-retinal相比,X射线结构显示了9-cis-retinal的独特结合口袋.
- 埋藏的水分子网络和Glu202被确定为关键的催化元件.
结论:
- CRALBP具有以前未知的热异构酶功能.
- 水分子在CRALBP的特异性和催化活性中起着至关重要的作用.
- 该研究提出了一种涉及CRALBP和水网的新型异构化机制.
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