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3J9W

Cryo-EM structure of the Bacillus subtilis MifM-stalled ribosome complex

This is a non-PDB format compatible entry.
Summary for 3J9W
Entry DOI10.2210/pdb3j9w/pdb
EMDB information6306
Descriptor16S ribosomal RNA, 30S ribosomal protein uS10, 30S ribosomal protein uS11, ... (54 entities in total)
Functional Keywordsstalling, translation arrest, mifm, l22, ribosome
Biological sourceBacillus subtilis subsp. subtilis str. 168
More
Total number of polymer chains54
Total formula weight2185398.95
Authors
Sohmen, D.,Chiba, S.,Shimokawa-Chiba, N.,Innis, C.A.,Berninghausen, O.,Beckmann, R.,Ito, K.,Wilson, D.N. (deposition date: 2015-03-16, release date: 2015-04-29, Last modification date: 2024-02-21)
Primary citationSohmen, D.,Chiba, S.,Shimokawa-Chiba, N.,Innis, C.A.,Berninghausen, O.,Beckmann, R.,Ito, K.,Wilson, D.N.
Structure of the Bacillus subtilis 70S ribosome reveals the basis for species-specific stalling.
Nat Commun, 6:6941-6941, 2015
Cited by
PubMed Abstract: Ribosomal stalling is used to regulate gene expression and can occur in a species-specific manner. Stalling during translation of the MifM leader peptide regulates expression of the downstream membrane protein biogenesis factor YidC2 (YqjG) in Bacillus subtilis, but not in Escherichia coli. In the absence of structures of Gram-positive bacterial ribosomes, a molecular basis for species-specific stalling has remained unclear. Here we present the structure of a Gram-positive B. subtilis MifM-stalled 70S ribosome at 3.5-3.9 Å, revealing a network of interactions between MifM and the ribosomal tunnel, which stabilize a non-productive conformation of the PTC that prevents aminoacyl-tRNA accommodation and thereby induces translational arrest. Complementary genetic analyses identify a single amino acid within ribosomal protein L22 that dictates the species specificity of the stalling event. Such insights expand our understanding of how the synergism between the ribosome and the nascent chain is utilized to modulate the translatome in a species-specific manner.
PubMed: 25903689
DOI: 10.1038/ncomms7941
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.9 Å)
Structure validation

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