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9P38

YsxC-GMPPNP treated 44.5SYsxC particles. Class 1.

Summary for 9P38
Entry DOI10.2210/pdb9p38/pdb
EMDB information71238
Descriptor23S rRNA, 50S ribosomal protein L21, 50S ribosomal protein L22, ... (18 entities in total)
Functional Keywordsribosome, 44.5s particle, ysxc
Biological sourceBacillus subtilis
More
Total number of polymer chains18
Total formula weight1174549.36
Authors
Ortega, J.,Seffouh, A. (deposition date: 2025-06-13, release date: 2025-11-12)
Primary citationSeffouh, A.,Arpin, D.,Basu, K.,Ortega, J.
YsxC is a placeholder for ribosomal protein uL2 during 50S ribosomal subunit assembly.
Nucleic Acids Res., 53:-, 2025
Cited by
PubMed Abstract: The maturation of the functional core of the 50S ribosomal subunit in Bacillus subtilis is assisted by assembly factors that enhance the efficiency of the process. Two essential assembly factors, the GTPases RbgA and YphC, bind at or near the functional sites of the 50S subunit to promote the folding of ribosomal RNA helices that play key functional roles. YsxC is another GTPase involved in the maturation of the 50S subunit, whose function remains unknown. We demonstrate that YsxC aids 50S assembly through a drastically different mechanism. YsxC binds in the body of the 44.5S large ribosome assembly intermediate, occupying the site where uL2 binds and controls the timing in the folding of rRNA helices forming the binding site for uL2. It creates a "primordial" binding site that includes six out of the eleven rRNA helices forming the uL2 mature binding site. Once YsxC is released, uL2 binds to this "primordial" binding site, and the remaining helices that stabilize uL2 fold, and the entire region adopts the mature conformation. This role of YsxC functioning as a placeholder factor for ribosomal protein uL2 provides the first example of such a factor's involvement in the ribosome assembly process in bacteria.
PubMed: 41148149
DOI: 10.1093/nar/gkaf1071
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.5 Å)
Structure validation

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