1H, 13C, 15N backbone and side-chain NMR assignments of the C-terminal domain of Mycobacterium Tuberculosis ribosome maturation factor RimM

Biomol NMR Assign. 2021 Oct;15(2):373-377. doi: 10.1007/s12104-021-10032-9. Epub 2021 Jun 8.

Abstract

Tuberculosis (TB), a lethal disease caused by Mycobacterium tuberculosis (Mtb) infection, develops multidrug-resistance and needs new drugs for effective treatment. As a ribosome maturation factor protein, RimM plays an essential role in the bacterial ribosome assembly and is a potential target for antibiotics against TB. RimM is involved in the incorporation of ribosomal protein S19 into the 30 S ribosomal subunit, where the C-terminal domain of RimM is speculated to bind S19. However, the structure and dynamics features of MtbRimM remain unclear to date. Herein, we report the NMR assignments for the 1H, 13C, 15N backbone and side-chain resonances of the C-terminal domain of MtbRimM. We also provide the prediction of its secondary structure and order parameters. Our work lays the basis for solution structure, dynamics and functional studies on MtbRimM in future, and provides clues for the anti-tuberculosis drug development.

Keywords: C-terminal domain; NMR resonance assignments; Ribosome maturation factor; RimM; Tuberculosis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Mycobacterium tuberculosis*