波谱学杂志 ›› 2012, Vol. 29 ›› Issue (2): 224-230.

• 研究论文 • 上一篇    下一篇

古菌蛋白质SSO6904的双体形式的NMR鉴定

姚宏伟1,2,冯银刚1,3*,王金凤1   

  1. 1. 中国科学院 生物物理研究所 生物大分子国家重点实验室,北京 100101; 
    2. 清华大学 生命科学学院,生物信息学教育部重点实验室,北京 100084;  3. 中国科学院 青岛生物能源与过程研究所,山东 青岛  266101
  • 收稿日期:2011-05-09 修回日期:2011-06-27 出版日期:2012-06-05 发布日期:2012-06-05
  • 基金资助:

    国家自然科学基金资助项目(30270301, 30770434).

Dimer Form of Archaeal Protein SSO6904 Identified by NMR

 YAO Hong-Wei1,2, FENG Yin-Gang1,3*, WANG Jin-Feng1   

  1. 1. State Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Science, Beijing 100101, China; 
    2. Key Laboratory of Bioinformatics of Ministry of Education, School of Life Sciences, Tsinghua University, Beijing 100084, China; 
    3. Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao 266101, China
  • Received:2011-05-09 Revised:2011-06-27 Online:2012-06-05 Published:2012-06-05
  • Supported by:

    国家自然科学基金资助项目(30270301, 30770434).

摘要:

古菌蛋白质SSO6904是最近发现的一个全螺旋结构的、具有弱的钙离子结合活性的蛋白质. 在蛋白质纯化过程中,通过凝胶过滤层析发现SSO6904具有稳定的单体和双体形式.  1H NMR谱表明2种形式的核心结构类似. 2D  1H-15N HSQC谱表明单体和双体的结构差异主要处在连接螺旋2和3以及5和6的2个Loop链接区域,这2个Loop链接区域是形成双体的关键区域,而其他区域具有相同的结构. 通过结构分析推测并搭建了一种结构域交换的SSO6904双体结构模型. 这种稳定的双体形式可能是调节SSO6904功能的一种方式.

关键词: 核磁共振(NMR), 蛋白质结构, HSQC, SSO6904, 古菌, 蛋白质双体

Abstract:

Archaeal protein SSO6904 is a newly-discovered protein with weak calcium-binding activity. Protein SSO6904 is an all-helices protein. Protein purification by gel filtration discovered both monomer and dimer forms of SSO6904. 1H NMR spectra indicated that the monomer and dimer have similar structural core. Analysis of 2D 1H-15N HSQC spectra revealed that the major structural difference between the monomer and dimer was at the two loops connecting helices 2 and 3, and helices 5 and 6, respectively. These two loops form a key structural region for constructing the dimer, while other regions of monomer and dimer have the same structures. Structural analysis proposed a domain-swapped model of the SSO6904 dimer. The domain-swapped dimer may regulate the stability and function of SSO6904.

Key words: NMR, protein structure, HSQC, SSO6904, archaea, protein dimer

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