2ZJR

Refined native structure of the large ribosomal subunit (50S) from Deinococcus radiodurans

Summary for 2ZJR

• Entry DOI: 10.2210/pdb2zjr/pdb
• Related: 2ZJP 2ZJQ 3CF5
• Descriptor: ribosomal 23S RNA, 50S ribosomal protein L14, 50S ribosomal protein L15, ... (31 entities in total)
• Functional Keywords: ribosome, large ribosomal subunit, 50s, ribonucleoprotein, ribosomal protein, rna-binding, rrna-binding, trna-binding, methylation, metal-binding, zinc-finger
• Biological source: Deinococcus radiodurans; More
• Total number of polymer chains: 30
• Total formula weight: 1365289.28

Authors

Harms, J.M.,Wilson, D.N.,Schluenzen, F.,Connell, S.R.,Stachelhaus, T.,Zaborowska, Z.,Spahn, C.M.T.,Fucini, P. (deposition date: 2008-03-08, release date: 2008-06-17, Last modification date: 2024-10-23)

Primary citation

Harms, J.M.,Wilson, D.N.,Schluenzen, F.,Connell, S.R.,Stachelhaus, T.,Zaborowska, Z.,Spahn, C.M.,Fucini, P.
Translational regulation via L11: molecular switches on the ribosome turned on and off by thiostrepton and micrococcin.
Mol.Cell, 30:26-38, 2008

PubMed Abstract: The thiopeptide class of antibiotics targets the GTPase-associated center (GAC) of the ribosome to inhibit translation factor function. Using X-ray crystallography, we have determined the binding sites of thiostrepton (Thio), nosiheptide (Nosi), and micrococcin (Micro), on the Deinococcus radiodurans large ribosomal subunit. The thiopeptides, by binding within a cleft located between the ribosomal protein L11 and helices 43 and 44 of the 23S rRNA, overlap with the position of domain V of EF-G, thus explaining how this class of drugs perturbs translation factor binding to the ribosome. The presence of Micro leads to additional density for the C-terminal domain (CTD) of L7, adjacent to and interacting with L11. The results suggest that L11 acts as a molecular switch to control L7 binding and plays a pivotal role in positioning one L7-CTD monomer on the G' subdomain of EF-G to regulate EF-G turnover during protein synthesis.

PubMed: 18406324
DOI: 10.1016/j.molcel.2008.01.009

Experimental method

X-RAY DIFFRACTION (2.91 Å)