Probing the pH sensitivity of R-phycoerythrin: Investigations of active conformational and functional variation
Probing the pH sensitivity of R-phycoerythrin: Investigations of active conformational and functional variation
复制标题
探讨 R-藻红蛋白的 pH 敏感性：活性构象和功能变异的研究
DOI：
10.1016/j.bbabio.2009.02.018
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发表时间：
2009-07-01
影响因子：
4.3
通讯作者：
Zhang, Yu-Zhong
中科院分区：
文献类型：
--
作者：
Liu, Lu-Ning;Su, Hai-Nan;Zhang, Yu-Zhong
藻胆蛋白的晶体结构提供了有关肽和发色团的构象和氨基酸组织的有价值的信息，并使我们能够研究它们的结构和功能与环境变化的关系。本文通过吸收光谱、荧光光谱、圆二色谱和晶体结构分析，研究了pH诱导的R-藻红蛋白（R-PE）的构象和功能动力学。与结构稳定性相比，R-PE在3.5-10的pH范围内具有更强的功能稳定性。超过这个范围，会发生明显的功能和结构变化。晶体结构分析表明，R-PE的三级结构是由蛋白质的几个关键锚定点固定的。通过这种特定的关联，R-PE的基本结构被稳定以呈现生理光谱特性，而蛋白质肽的局部变化也被允许响应环境干扰。R-PE的功能稳定性和相对结构敏感性允许环境适应。(C)2009 Elsevier B. V.保留所有权利。
Crystal structures of phycobiliproteins have provided valuable information regarding the conformations and amino acid organizations of peptides and chromophores, and enable us to investigate their structural and functional relationships with respect to environmental variations. In this work, we explored the pH-induced conformational and functional dynamics of R-phycoerythrin (R-PE) by means of absorption, fluorescence and circular dichroism spectra, together with analysis of its crystal structure. R-PE presents stronger functional stability in the pH range of 3.5-10 compared to the structural stability. Beyond this range, pronounced functional and structural changes occur. Crystal structure analysis shows that the tertiary structure of R-PE is fixed by several key anchoring points of the protein. With this specific association, the fundamental structure of R-PE is stabilized to present physiological spectroscopic properties, while local variations in protein peptides are also allowed in response to environmental disturbances. The functional stability and relative structural sensitivity of R-PE allow environmental adaptation. (C) 2009 Elsevier B.V. All rights reserved.