Sequence specific 1H, 13C and 15N backbone resonance assignments of UVI31+from Chlamydomonas reinhardtii
Sequence specific 1H, 13C and 15N backbone resonance assignments of UVI31+from Chlamydomonas reinhardtii
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DOI：
10.1007/s12104-010-9239-4
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发表时间：
2010-10-01
影响因子：
0.9
通讯作者：
Chary, K. V. R.
中科院分区：
文献类型：
--
作者：
Rout, Ashok K.;Minda, R.;Chary, K. V. R.
从C. reinhardtii，并在E.大肠杆菌中纯化蛋白质至均一。纯化的蛋白质表现出β-内酰胺酶活性（Mandarin在制备中）。然而，UVI 31+与已知的β-内酰胺酶没有同源性。为了理解UVI 31+水解β-内酰胺抗生素的能力的结构基础，我们同时着手通过NMR对其进行结构表征。其β-内酰胺酶活性与溶液结构（NMR）的关系可能会加深对其机制的理解，并促进蛋白质其他功能（如果有的话）的合理化。在这项奋进中，我们报告了几乎完整的序列特异性骨架H-1，C-13和N-15 NMR分配的UVI 31+。
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 beta-lactamases. In order to understand the structural basis of the ability of UVI31+ to hydrolyze beta-lactam antibiotics, we in parallel, set out to structurally characterize it by NMR. Its beta-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 H-1, C-13 and N-15 NMR assignments of UVI31+.