High Resolution Structure of the Large Ribosomal Subunit from a Mesophilic Eubacterium
| Autor: | Frank Schluenzen, Joerg Harms, Raz Zarivach, Sharon Gat, Heike Bartels, Anat Bashan, Ilana Agmon, Ada Yonath, Francois Franceschi |
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| Rok vydání: | 2001 |
| Předmět: |
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Molecular Ribosomal Proteins Macromolecular Substances Protein Conformation Biology Crystallography X-Ray Ribosome Protein Structure Secondary General Biochemistry Genetics and Molecular Biology 03 medical and health sciences Bacterial Proteins RNA Transfer Ribosomal protein Large ribosomal subunit Eukaryotic Small Ribosomal Subunit 030304 developmental biology 50S 0303 health sciences Molecular Structure Eukaryotic Large Ribosomal Subunit Biochemistry Genetics and Molecular Biology(all) 030302 biochemistry & molecular biology Ribosomal RNA Protein Structure Tertiary Gram-Positive Cocci RNA Bacterial Biochemistry RNA Ribosomal Transfer RNA Nucleic Acid Conformation Ribosomes |
| Zdroj: | Cell. 107(5):679-688 |
| ISSN: | 0092-8674 |
| DOI: | 10.1016/s0092-8674(01)00546-3 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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