The complete atomic structure of the large ribosomal subunit at 2.4 A resolution.
Science
; 289(5481): 905-20, 2000 Aug 11.
Article
em En
| MEDLINE
| ID: mdl-10937989
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas Ribossômicas
/
Ribossomos
/
RNA Ribossômico 5S
/
RNA Ribossômico 23S
/
Haloarcula marismortui
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
Science
Ano de publicação:
2000
Tipo de documento:
Article
País de afiliação:
Estados Unidos