7BOD

Bacterial 30S ribosomal subunit assembly complex state M (body domain)

Summary for 7BOD

• Entry DOI: 10.2210/pdb7bod/pdb
• EMDB information: 12239
• Descriptor: 16S rRNA (body domain of 30S subunit), 30S ribosomal protein S17, 30S ribosomal protein S18, ... (14 entities in total)
• Functional Keywords: cryo-em, 30s biogenesis, ribosome assembly, rbfa, rsga, yjeq, rimp, ksga, rsma, ribosome
• Biological source: Escherichia coli (strain K12); More
• Total number of polymer chains: 13
• Total formula weight: 657491.96

Authors

Schedlbauer, A.,Iturrioz, I.,Ochoa-Lizarralde, B.,Diercks, T.,Lopez-Alonso, J.,Kaminishi, T.,Capuni, R.,Astigarraga, E.,Gil-Carton, D.,Fucini, P.,Connell, S.R. (deposition date: 2021-01-25, release date: 2021-07-07, Last modification date: 2024-04-24)

Primary citation

Schedlbauer, A.,Iturrioz, I.,Ochoa-Lizarralde, B.,Diercks, T.,Lopez-Alonso, J.P.,Lavin, J.L.,Kaminishi, T.,Capuni, R.,Dhimole, N.,de Astigarraga, E.,Gil-Carton, D.,Fucini, P.,Connell, S.R.
A conserved rRNA switch is central to decoding site maturation on the small ribosomal subunit.
Sci Adv, 7:-, 2021

PubMed Abstract: While a structural description of the molecular mechanisms guiding ribosome assembly in eukaryotic systems is emerging, bacteria use an unrelated core set of assembly factors for which high-resolution structural information is still missing. To address this, we used single-particle cryo-electron microscopy to visualize the effects of bacterial ribosome assembly factors RimP, RbfA, RsmA, and RsgA on the conformational landscape of the 30 ribosomal subunit and obtained eight snapshots representing late steps in the folding of the decoding center. Analysis of these structures identifies a conserved secondary structure switch in the 16 ribosomal RNA central to decoding site maturation and suggests both a sequential order of action and molecular mechanisms for the assembly factors in coordinating and controlling this switch. Structural and mechanistic parallels between bacterial and eukaryotic systems indicate common folding features inherent to all ribosomes.

PubMed: 34088665
DOI: 10.1126/sciadv.abf7547

Experimental method

ELECTRON MICROSCOPY (2.88 Å)