3CF5

Thiopeptide antibiotic Thiostrepton bound to the large ribosomal subunit of Deinococcus radiodurans

Summary for 3CF5

• Entry DOI: 10.2210/pdb3cf5/pdb
• Related: 1D8T 1E9W 1OLN 2C77 2JQ7 2ZJP
• Related PRD ID: PRD_000223
• Descriptor: 50S RIBOSOMAL PROTEIN L33, 50S RIBOSOMAL PROTEIN L6, 50S RIBOSOMAL PROTEIN L11, ... (32 entities in total)
• Functional Keywords: ribosome-antibiotic complex, antibiotic, ribosome, thiostrepton, rna, l11, thiopeptide, thiazole, thiazoline, pyridine, translation inhibition, ribosome/antibiotic
• Biological source: DEINOCOCCUS RADIODURANS; More
• Total number of polymer chains: 31
• Total formula weight: 1367119.57

Authors

Harms, J.M.,Wilson, D.N.,Schluenzen, F.,Connell, S.R.,Stachelhaus, T.,Zaborowska, Z.,Spahn, C.M.T.,Fucini, P. (deposition date: 2008-03-02, release date: 2008-06-17, Last modification date: 2023-11-15)

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-, 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 (3.3 Å)