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TitleHigh resolution structure of the large ribosomal subunit from a mesophilic eubacterium.
Journal, issue, pagesCell, Vol. 107, Issue 5, Page 679-688, Year 2001
Publish dateNov 30, 2001
AuthorsJ Harms / F Schluenzen / R Zarivach / A Bashan / S Gat / I Agmon / H Bartels / F Franceschi / A Yonath /
PubMed AbstractWe describe the high resolution structure of the large ribosomal subunit from Deinococcus radiodurans (D50S), a gram-positive mesophile suitable for binding of antibiotics and functionally relevant ...We describe the high resolution structure of the large ribosomal subunit from Deinococcus radiodurans (D50S), a gram-positive mesophile suitable for binding of antibiotics and functionally relevant ligands. The over-all structure of D50S is similar to that from the archae bacterium Haloarcula marismortui (H50S); however, a detailed comparison revealed significant differences, for example, in the orientation of nucleotides in peptidyl transferase center and in the structures of many ribosomal proteins. Analysis of ribosomal features involved in dynamic aspects of protein biosynthesis that are partially or fully disordered in H50S revealed the conformations of intersubunit bridges in unbound subunits, suggesting how they may change upon subunit association and how movements of the L1-stalk may facilitate the exit of tRNA.
External linksCell / PubMed:11733066
MethodsX-ray diffraction
Resolution3.1 Å
Structure data

PDB-1nkw:
Crystal Structure Of The Large Ribosomal Subunit From Deinococcus Radiodurans
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

Source
  • deinococcus radiodurans (radioresistant)
KeywordsRIBOSOME / Ribosome; large subunit; 50S; Deinococcus Radiodurans; X-ray structure; peptidyl-transferase / peptide bond formation

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