The Complete Atomic Structure of the Large Ribosomal Subunit at 2.4 Å Resolution

TLDR

The large ribosomal subunit catalyzes peptide bond formation, binds translation factors, and its RNA domains assemble into a monolithic structure stabilized by surface proteins that interact with multiple RNA domains, except at the active site where peptide bond formation occurs. The crystal structure of the Haloarcula marismortui large ribosomal subunit was solved at 2.4 Å, revealing 2833 of 3045 nucleotides and 27 of 31 proteins.

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.