Abstract
We report the NMR resonance assignments of N-terminal signal sequence deleted secretory protein Rv0603 (∆1–28−Rv0603) from Mycobacterium tuberculosis H37Rv. ∆1–28−Rv0603 displayed good peak yield and signal dispersion in 2D [15N-1H] HSQC spectrum, which prompted us to proceed for resonance assignments on this construct. Standard triple-resonance experiments for resonance assignments were recorded on [U-15N]-∆Rv0603 and [U-15N, 13C]-∆Rv0603 samples. We obtained 97% of backbone 1HN, 98% of 13Cα, 98% of 1Hα, 96% of 13C´, 100% of 13Cβ, 100% of 1Hβ and 98% of side-chain 1H 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.
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Acknowledgements
This work was supported by grant EMR/2016/005365 from DST, India. S.T. is grateful to School of Chemistry, Sambalpur University for her PhD registration. This is communication number 10052 from CSIR-CDRI.
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Tripathi, S., Yadav, R., Jain, A. et al. Resonance assignments and secondary structure prediction of secretory protein Rv0603 from Mycobacterium tuberculosis H37Rv. Biomol NMR Assign 14, 217–219 (2020). https://doi.org/10.1007/s12104-020-09948-5
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DOI: https://doi.org/10.1007/s12104-020-09948-5