High resolution structure of the large ribosomal subunit from a mesophilic eubacterium

Joerg Harms, Frank Schluenzen, Raz Zarivach, Anat Bashan, Sharon Gat, Ilana Agmon, Heike Bartels, François Franceschi, Ada Yonath

Research output: Contribution to journalArticlepeer-review

762 Scopus citations

Abstract

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 overall 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 tRNA.

Original languageEnglish
Pages (from-to)679-688
Number of pages10
JournalCell
Volume107
Issue number5
DOIs
StatePublished - 30 Nov 2001
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology (all)

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