Abstract

The large ribosomal subunit catalyzes peptide bond formation and binds initiation, termination, and elongation factors. We have determined the crystal structure of the large ribosomal subunit from Haloarcula marismortui at 2.4 angstrom resolution, and it includes 2833 of the subunit's 3045 nucleotides and 27 of its 31 proteins. The domains of its RNAs all have irregular shapes and fit together in the ribosome like the pieces of a three-dimensional jigsaw puzzle to form a large, monolithic structure. Proteins are abundant everywhere on its surface except in the active site where peptide bond formation occurs and where it contacts the small subunit. Most of the proteins stabilize the structure by interacting with several RNA domains, often using idiosyncratically folded extensions that reach into the subunit's interior.

Keywords

RibosomeProtein subunitRibosomal proteinRibosomal RNAEukaryotic RibosomeCrystallographyResolution (logic)Eukaryotic Large Ribosomal SubunitChemistryRNABiologyBiophysicsBiochemistry

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Publication Info

Year
2000
Type
article
Volume
289
Issue
5481
Pages
905-920
Citations
3269
Access
Closed

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Nenad Ban, Poul Nissen, J.L. Hansen et al. (2000). The Complete Atomic Structure of the Large Ribosomal Subunit at 2.4 Å Resolution. Science , 289 (5481) , 905-920. https://doi.org/10.1126/science.289.5481.905

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DOI
10.1126/science.289.5481.905