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 (1)H, (13)C and (15)N NMR assignments of UVI31+.
journal_name
Biomol NMR Assignjournal_title
Biomolecular NMR assignmentsauthors
Rout AK,Minda R,Peri D,Ramakrishnan V,Bhattacharjee SK,Rao BJ,Chary KVdoi
10.1007/s12104-010-9239-4subject
Has Abstractpub_date
2010-10-01 00:00:00pages
171-4issue
2eissn
1874-2718issn
1874-270Xjournal_volume
4pub_type
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