结核分枝杆菌 H37Rv 分泌蛋白 Rv0603 的共振分配和二级结构预测。
Resonance assignments and secondary structure prediction of secretory protein Rv0603 from Mycobacterium tuberculosis H37Rv.
机构信息
Molecular and Structural Biology Division, CSIR-Central Drug Research Institute, Lucknow, Uttar Pradesh, 226 031, India.
School of Chemistry, Sambalpur University, Jyoti Vihar, Sambalpur, Odisha, 768019, India.
出版信息
Biomol NMR Assign. 2020 Oct;14(2):217-219. doi: 10.1007/s12104-020-09948-5. Epub 2020 May 20.
We report the NMR resonance assignments of N-terminal signal sequence deleted secretory protein Rv0603 (∆-Rv0603) from Mycobacterium tuberculosis H37Rv. ∆-Rv0603 displayed good peak yield and signal dispersion in 2D [N-H] HSQC spectrum, which prompted us to proceed for resonance assignments on this construct. Standard triple-resonance experiments for resonance assignments were recorded on [U-N]-∆Rv0603 and [U-N, C]-∆Rv0603 samples. We obtained 97% of backbone H, 98% of C, 98% of H, 96% of C´, 100% of C, 100% of H and 98% of side-chain H chemical shifts. This protein does not show any sequence similarity to any other protein of known structure. Determination of its solution structure would facilitate understanding of its biological function.
我们报道了来自结核分枝杆菌 H37Rv 的 N 端信号序列缺失分泌蛋白 Rv0603（∆-Rv0603）的 NMR 共振峰分配。∆-Rv0603 在 2D [N-H] HSQC 谱中显示出良好的峰产量和信号分散性，这促使我们对该结构进行共振峰分配。标准的三重共振实验用于共振峰分配在 [U-N]-∆Rv0603 和 [U-N, C]-∆Rv0603 样品上进行。我们得到了 97%的骨架 H、98%的 C、98%的 H、96%的 C´、100%的 C、100%的 H 和 98%的侧链 H 化学位移。该蛋白与任何已知结构的其他蛋白均无序列相似性。确定其溶液结构将有助于理解其生物学功能。
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