Yao Chendie, Wu Qiong, Xu Guohua, Li Conggang
Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan, Wuhan Institute of Physics and Mathematics, Chinese Academy of Sciences, Wuhan, 430071, People's Republic of China.
Biomol NMR Assign. 2017 Oct;11(2):239-242. doi: 10.1007/s12104-017-9756-5. Epub 2017 Aug 14.
The emerging of the New Delhi metallo-beta-lactamase (NDM-1) has become one of the greatest threats to the clinical treatment. Although the structure of NDM-1 has been determined by X-ray crystallography, the molecular mechanism and process of catalysis reaction remain elusive. NMR spectroscopy plays a unique role in the characterization of conformational dynamics. Here we report the backbone H, N and C chemical shift assignments of NDM-1 by heteronuclear multidimensional NMR spectroscopy as well as its secondary structure in solution as predicted by TALOS+.
新德里金属β-内酰胺酶（NDM-1）的出现已成为临床治疗面临的最大威胁之一。尽管NDM-1的结构已通过X射线晶体学确定，但其催化反应的分子机制和过程仍不清楚。核磁共振光谱在构象动力学表征中发挥着独特作用。在此，我们报告了通过异核多维核磁共振光谱对NDM-1主链H、N和C化学位移的归属，以及通过TALOS+预测的其在溶液中的二级结构。
