Biomolecular NMR Assignments

, Volume 4, Issue 2, pp 171–174

Sequence specific 1H, 13C and 15N backbone resonance assignments of UVI31+ from Chlamydomonas reinhardtii

  • Ashok K. Rout
  • R. Minda
  • D. Peri
  • V. Ramakrishnan
  • S. K. Bhattacharjee
  • B. J. Rao
  • K. V. R. Chary
Article

DOI: 10.1007/s12104-010-9239-4

Cite this article as:
Rout, A.K., Minda, R., Peri, D. et al. Biomol NMR Assign (2010) 4: 171. doi:10.1007/s12104-010-9239-4

Abstract

The cDNA of UVI31+ was cloned from C. reinhardtii and expressed in E. coli from where the protein was purified to homogeneity. The purified protein exhibited beta-lactamase activity (Manuscript in preparation). However, UVI31+ has no homology with the known β-lactamases. In order to understand the structural basis of the ability of UVI31+ to hydrolyze β-lactam antibiotics, we in parallel, set out to structurally characterize it by NMR. Its β-lactamase activity in relation to the solution structure by NMR is likely to provoke deeper understanding of its mechanism and facilitate the rationalization of other functions of the protein, if any. In this endeavor, we report almost complete sequence-specific backbone 1H, 13C and 15N NMR assignments of UVI31+.

Keywords

NMR Resonance assignments Triple resonance experiments UVI31+ Chlamydomonas reinhardtii Green alga 

Copyright information

© Springer Science+Business Media B.V. 2010

Authors and Affiliations

  • Ashok K. Rout
    • 1
  • R. Minda
    • 1
  • D. Peri
    • 2
  • V. Ramakrishnan
    • 1
  • S. K. Bhattacharjee
    • 2
    • 3
  • B. J. Rao
    • 2
  • K. V. R. Chary
    • 1
  1. 1.Department of Chemical SciencesTata Institute of Fundamental ResearchColaba, MumbaiIndia
  2. 2.Department of Biological SciencesTata Institute of Fundamental ResearchMumbaiIndia
  3. 3.School of Life SciencesDevi Ahilya VishwavidyalayaIndoreIndia