2otl
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Girodazole bound to the large subunit of Haloarcula marismortui
OverviewOverview
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.
About this StructureAbout this Structure
2OTL is a Protein complex structure of sequences from Haloarcula marismortui with GIR, MG, K, NA, CD and CL as ligands. Full crystallographic information is available from OCA.
ReferenceReference
The Structures of Antibiotics Bound to the E Site Region of the 50 S Ribosomal Subunit of Haloarcula marismortui: 13-Deoxytedanolide and Girodazole., Schroeder SJ, Blaha G, Tirado-Rives J, Steitz TA, Moore PB, J Mol Biol. 2007 Apr 13;367(5):1471-9. Epub 2007 Feb 7. PMID:17321546
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