1FFK

CRYSTAL STRUCTURE OF THE LARGE RIBOSOMAL SUBUNIT FROM HALOARCULA MARISMORTUI AT 2.4 ANGSTROM RESOLUTION

Summary for 1FFK

• Entry DOI: 10.2210/pdb1ffk/pdb
• Related: 1c04
• Descriptor: 23S RRNA, RIBOSOMAL PROTEIN L14, RIBOSOMAL PROTEIN L15E, ... (33 entities in total)
• Functional Keywords: ribosome assembly, rna-rna, protein-rna, protein-protein, ribosome
• Biological source: Haloarcula marismortui; More
• Total number of polymer chains: 29
• Total formula weight: 1404958.21

Authors

Ban, N.,Nissen, P.,Hansen, J.,Moore, P.B.,Steitz, T.A. (deposition date: 2000-07-25, release date: 2000-08-14, Last modification date: 2024-02-07)

Primary citation

Ban, N.,Nissen, P.,Hansen, J.,Moore, P.B.,Steitz, T.A.
The complete atomic structure of the large ribosomal subunit at 2.4 A resolution.
Science, 289:905-920, 2000

PubMed 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.

PubMed: 10937989
DOI: 10.1126/science.289.5481.905

Experimental method

X-RAY DIFFRACTION (2.4 Å)