Sequence specific 1H, 13C and 15N backbone resonance assignments of UVI31+ from Chlamydomonas reinhardtii.
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 (1)H, (13)C and (15)N NMR assignments of UVI31+.
Department of Chemical Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Colaba, Mumbai, 400005, India.
Ashok K
AK
Rout
R
R
Minda
D
D
Peri
V
V
Ramakrishnan
S K
SK
Bhattacharjee
B J
BJ
Rao
K V R
KV
Chary
D000595:Amino Acid Sequence; D002247:Carbon Isotopes; D016825:Chlamydomonas reinhardtii / Q000737:chemistry*; D006859:Hydrogen; D006863:Hydrogen-Ion Concentration; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D010940:Plant Proteins / Q000737:chemistry*; D017433:Protein Structure, Secondary
D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D010940:Plant Proteins; D006859:Hydrogen