9XW3

CspB from Mycobacterium tuberculosis

Summary for 9XW3

• Entry DOI: 10.2210/pdb9xw3/pdb
• Descriptor: Probable cold shock-like protein B CspB (1 entity in total)
• Functional Keywords: rna chaperon, csp, mycobacterium tuberculosis, rna-binding protein, rna binding protein
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 1
• Total formula weight: 14914.87

Authors

Nikulin, A.D.,Lekontseva, N.V.,Pankratova, P.Y. (deposition date: 2025-11-27, release date: 2026-01-21, Last modification date: 2026-02-18)

Primary citation

Lekontseva, N.,Mikhaylina, A.,Pankratova, P.,Nikulin, A.
The Cold Shock Protein CspB from Mycobacterium tuberculosis Binds to MTS0997 sRNA and MTS1338 sRNA as a Dimer.
Int J Mol Sci, 27:-, 2026

PubMed Abstract: RNA chaperones play a crucial role in the biogenesis and function of various RNAs in bacteria. They facilitate the interaction of small regulatory trans-encoded sRNAs with mRNAs, thereby significantly altering the pattern of gene expression in cells. This allows bacteria to respond quickly to changing environmental conditions, such as stress or adaptation to host organisms. Despite the identification of a large number of sRNAs in mycobacteria, none of the most common RNA chaperones have been found in their genomes. We determined the crystal structure of the cold shock protein CspB from . It forms a dimer due to its elongated C-terminal region, which is a hairpin composed of two α-helices. It was also demonstrated that CspB from exhibits high affinity for MTS0997 sRNA and MTS1338 sRNA from the same organism, which is consistent with classical RNA chaperons such as Hfq and ProQ. Based on the putative RNA chaperone activity of bacterial proteins with cold-shock domains, we propose that CspB from may be involved in the regulation of mycobacterial pathogenesis through interaction with sRNAs.

PubMed: 41596314
DOI: 10.3390/ijms27020663

Experimental method

X-RAY DIFFRACTION (3.6 Å)