The thermal adaptation of the nitrogenase Fe protein from thermophilic Methanobacter thermoautotrophicus.
The thermal adaptation of the nitrogenase Fe protein from thermophilic Methanobacter thermoautotrophicus.
复制标题
嗜热甲烷杆菌热自养固氮酶 Fe 蛋白的热适应。
DOI：
10.1002/prot.20765
复制
发表时间：
2006
期刊：
影响因子：
--
通讯作者：
Peters,JohnW
中科院分区：
文献类型：
--
作者：
Sen,Sanchayita;Peters,JohnW
固氮酶铁蛋白是生物固氮过程中生化机械的关键组成部分。铁蛋白是一类核苷酸结合蛋白的成员，它将核苷三磷酸的结合和水解与构象变化结合在一起。依赖核苷酸的构象变化调节大分子复合体的形成，这类成员包括Gα、EF-Tu和肌球蛋白。这一类的成员是非常有趣的模型系统，用于分析热适应性的各个方面，因为它们的机制涉及蛋白质构象变化和蛋白质-蛋白质相互作用。在这项研究中，我们利用我们对多种结构构象中的棕色固氮菌和二氨基固氮酶Fe蛋白结构的广泛知识，并使用标准的同源建模方法来建立相似结构构象中嗜热甲烷自养杆菌的Fe蛋白的可靠模型。由此产生的结构比较表明，它们的热适应。热自养铁蛋白是由许多因素引起的，包括蛋白质内部的各种结构变化导致的结构刚性增加。对假想的对接模型和固氮酶复合体结构的分析为蛋白质-蛋白质相互作用的热适应提供了见解，这些相互作用支持大分子复合体的形成和在更高温度下的催化。蛋白质2006年。©2005 Wiley-Liss Inc.
The nitrogenase Fe protein is a key component of the biochemical machinery responsible for the process of biological nitrogen fixation. The Fe protein is a member of a class of nucleotide‐binding proteins that couple the binding and hydrolysis of nucleoside triphosphates to conformational changes. The nucleotide‐dependent conformational changes modulate the formation of a macromolecular complex, and some members of the class include Gα, EF‐Tu, and myosin. The members of this class are highly interesting model systems for the analysis of aspects of thermal adaptability, since their mechanisms involve protein conformational change and protein–protein interactions. In this study, we have used our extensive knowledge of the structure of theAzotobacter vinelandiinitrogenase Fe protein in multiple structural conformations, and standard homology modeling approaches have been used to generate reliable models of the Fe protein from thermophilicMethanobacter thermoautotrophicusin the analogous structural conformations. The resulting structural comparison reveals that thermal adaptation of theM. thermoautotrophicusFe protein is conferred by a number of factors, including increased structural rigidity that results from various structural changes within the protein interior. The analysis of hypothetical docking models and nitrogenase complex structures provides insights into the thermal adaptation of the protein–protein interactions that support macromolecular complex formation and catalysis at higher temperatures. Proteins 2006. © 2005 Wiley‐Liss, Inc.