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2OTL

Girodazole bound to the large subunit of Haloarcula marismortui

Summary for 2OTL
Entry DOI10.2210/pdb2otl/pdb
Related2OTJ
Descriptor23S ribosomal RNA, 50S ribosomal protein L10e, 50S ribosomal protein L13P, ... (38 entities in total)
Functional Keywordsgirodazole, girolline, antibiotic complex, 50s, ribosome, large subunit
Biological sourceHaloarcula marismortui
More
Cellular locationCytoplasm : P12743
Total number of polymer chains31
Total formula weight1478307.14
Authors
Blaha, G.,Schroeder, S.J.,Tirado-Rives, J. (deposition date: 2007-02-08, release date: 2007-04-03, Last modification date: 2024-11-13)
Primary citationSchroeder, S.J.,Blaha, G.,Tirado-Rives, J.,Steitz, T.A.,Moore, P.B.
The Structures of Antibiotics Bound to the E Site Region of the 50 S Ribosomal Subunit of Haloarcula marismortui: 13-Deoxytedanolide and Girodazole.
J.Mol.Biol., 367:1471-1479, 2007
Cited by
PubMed Abstract: Crystal structures of the 50 S ribosomal subunit from Haloarcula marismortui complexed with two antibiotics have identified new sites at which antibiotics interact with the ribosome and inhibit protein synthesis. 13-Deoxytedanolide binds to the E site of the 50 S subunit at the same location as the CCA of tRNA, and thus appears to inhibit protein synthesis by competing with deacylated tRNAs for E site binding. Girodazole binds near the E site region, but is somewhat buried and may inhibit tRNA binding by interfering with conformational changes that occur at the E site. The specificity of 13-deoxytedanolide for eukaryotic ribosomes is explained by its extensive interactions with protein L44e, which is an E site component of archaeal and eukaryotic ribosomes, but not of eubacterial ribosomes. In addition, protein L28, which is unique to the eubacterial E site, overlaps the site occupied by 13-deoxytedanolide, precluding its binding to eubacterial ribosomes. Girodazole is specific for eukarytes and archaea because it makes interactions with L15 that are not possible in eubacteria.
PubMed: 17321546
DOI: 10.1016/j.jmb.2007.01.081
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

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