Rout, Ashok K. ; Minda, R. ; Peri, D. ; Ramakrishnan, V. ; Bhattacharjee, S. K. ; Rao, B. J. ; Chary, K. V. R. (2010) Sequence specific 1H, 13C and 15N backbone resonance assignments of UVI31+ from Chlamydomonas reinhardtii Biomolecular NMR Assignments, 4 (2). pp. 171-174. ISSN 1874 2718
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Official URL: http://link.springer.com/article/10.1007%2Fs12104-...
Related URL: http://dx.doi.org/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+.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to Springer Verlag. |
| Keywords: | NMR; Resonance Assignments; Triple Resonance Experiments; UVI31+ Chlamydomonas reinhardtii; Green Alga |
| ID Code: | 107049 |
| Deposited On: | 15 Jun 2017 10:53 |
| Last Modified: | 15 Jun 2017 10:53 |
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