6TG6

Toprim domain of RNase M5

Summary for 6TG6

• Entry DOI: 10.2210/pdb6tg6/pdb
• Descriptor: Ribonuclease M5 (2 entities in total)
• Functional Keywords: rnase m5, rnase, rrna, 5s rrna, precursor rrna, pre-5s rrna, ribosomal rna, ribonuclease, catalytic domain, toprim domain, hydrolase
• Biological source: Geobacillus stearothermophilus
• Total number of polymer chains: 1
• Total formula weight: 12528.24

Authors

Oerum, S.,Catala, M.,Tisne, C. (deposition date: 2019-11-15, release date: 2020-09-23, Last modification date: 2024-05-01)

Primary citation

Oerum, S.,Dendooven, T.,Catala, M.,Gilet, L.,Degut, C.,Trinquier, A.,Bourguet, M.,Barraud, P.,Cianferani, S.,Luisi, B.F.,Condon, C.,Tisne, C.
Structures of B. subtilis Maturation RNases Captured on 50S Ribosome with Pre-rRNAs.
Mol.Cell, 80:227-, 2020

PubMed Abstract: The pathways for ribosomal RNA (rRNA) maturation diverge greatly among the domains of life. In the Gram-positive model bacterium, Bacillus subtilis, the final maturation steps of the two large ribosomal subunit (50S) rRNAs, 23S and 5S pre-rRNAs, are catalyzed by the double-strand specific ribonucleases (RNases) Mini-RNase III and RNase M5, respectively. Here we present a protocol that allowed us to solve the 3.0 and 3.1 Å resolution cryoelectron microscopy structures of these RNases poised to cleave their pre-rRNA substrates within the B. subtilis 50S particle. These data provide the first structural insights into rRNA maturation in bacteria by revealing how these RNases recognize and process double-stranded pre-rRNA. Our structures further uncover how specific ribosomal proteins act as chaperones to correctly fold the pre-rRNA substrates and, for Mini-III, anchor the RNase to the ribosome. These r-proteins thereby serve a quality-control function in the process from accurate ribosome assembly to rRNA processing.

PubMed: 32991829
DOI: 10.1016/j.molcel.2020.09.008

Experimental method

X-RAY DIFFRACTION (1.3 Å)