8YEQ

Crystal structure of L7/L12 Ribosomal Protein from Mycobacterium tuberculosis

Summary for 8YEQ

• Entry DOI: 10.2210/pdb8yeq/pdb
• Descriptor: Large ribosomal subunit protein bL12, 1,2-ETHANEDIOL (3 entities in total)
• Functional Keywords: ribosomal protein, single crystal, structural protein, translational protein
• Biological source: Mycobacterium tuberculosis CDC1551
• Total number of polymer chains: 1
• Total formula weight: 18245.90

Authors

Panicker, L.,Tripathi, P. (deposition date: 2024-02-23, release date: 2024-09-04, Last modification date: 2025-06-18)

Primary citation

Tripathi, P.,Panicker, L.
Crystal structure, biophysical characterisation, modeling and docking studies of bL12 ribosomal protein from Mycobacterium tuberculosis.
Arch.Biochem.Biophys., 771:110489-110489, 2025

PubMed Abstract: Tuberculosis (TB) is a fatal infectious disease caused by Mycobacterium tuberculosis (Mtb), with high rates of relapse and mortality worldwide. The Mtb stalk protein bL7/bL12 is a component of 50S ribosomal subunit, and plays a crucial role in the translation process during protein synthesis. The bL7 differs from bL12 by the presence of an acetyl group at its N-terminal region. In this study, the bL12 gene from Mtb was cloned into prokaryotic expression vector pET-28a(+), then expressed, purified, characterised and crystallised using the vapour diffusion method. Rod-shaped crystals of bL12 were obtained, which diffracted to 1.5 Å resolution at 100 K, with an R of 0.025. The bL12 crystallised in the P222 space group with unit cell dimensions a = 25.86 Å, b = 47.27 Å, c = 61.07 Å, and α = β = γ = 90°. The compact, globular C-terminal domain consists of β1-α1-α2-β2-α3-β3 fold. The bL12 protein was further characterised using various biophysical techniques: CD, SEC, DLS, DSC, DSF and fluorescence spectroscopy. Structural modeling and docking of bL12 protein with its interacting partners in the ribosome were performed using HDOCK and AlphaFold3. The resulting data were analysed to gain insights into its functional role. This structural information on the Mtb bL12 protein enhances our understanding of translational biology and contributes to structure-based drug design efforts targeting tuberculosis.

PubMed: 40466900
DOI: 10.1016/j.abb.2025.110489

Experimental method

X-RAY DIFFRACTION (1.5 Å)