Chinese Journal of Magnetic Resonance ›› 2012, Vol. 29 ›› Issue (2): 224-230.

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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).

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

CLC Number: