2otl
From Proteopedia
Girodazole bound to the large subunit of Haloarcula marismortui
Overview
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 Structure
2OTL is a Protein complex structure of sequences from Haloarcula marismortui. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sun May 4 11:37:47 2008
