Resonance assignments and secondary structure prediction of secretory protein Rv0603 from Mycobacterium tuberculosis H37Rv

• Published in: Biomolecular NMR assignments Vol. 14; no. 2; pp. 217 - 219
• Main Authors: Tripathi, Sarita, Yadav, Rahul, Jain, Anupam, Pulavarti, Surya V. S. R. K., Pathak, Prem Prakash, Behera, Ajaya Kumar, Arora, Ashish
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer Netherlands 01.10.2020; Springer Nature B.V
• Subjects: Amino acid sequence; Biochemistry; Biological and Medical Physics; Biophysics; Mycobacterium tuberculosis; NMR; Nuclear magnetic resonance; Physics; Physics and Astronomy; Polymer Sciences; Protein structure; Proteins; Secondary structure; Tuberculosis; Resonance assignment; Secreted protein; NMR; ∆; Rv0603; 1–28−Rv0603
• ISSN: 1874-2718; 1874-270X
• DOI: 10.1007/s12104-020-09948-5

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 [ 15 N- 1 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 - 15 N]-∆Rv0603 and [ U - 15 N, 13 C]-∆Rv0603 samples. We obtained 97% of backbone 1 H N , 98% of 13 C α , 98% of 1 H α , 96% of 13 C´, 100% of 13 C β , 100% of 1 H β and 98% of side-chain 1 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.