Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 A resolution.
Nature
; 417(6890): 712-9, 2002 Jun 13.
Article
en En
| MEDLINE
| ID: mdl-12000971
ABSTRACT
In bacteria, the binding of a single protein, the initiation factor sigma, to a multi-subunit RNA polymerase core enzyme results in the formation of a holoenzyme, the active form of RNA polymerase essential for transcription initiation. Here we report the crystal structure of a bacterial RNA polymerase holoenzyme from Thermus thermophilus at 2.6 A resolution. In the structure, two amino-terminal domains of the sigma subunit form a V-shaped structure near the opening of the upstream DNA-binding channel of the active site cleft. The carboxy-terminal domain of sigma is near the outlet of the RNA-exit channel, about 57 A from the N-terminal domains. The extended linker domain forms a hairpin protruding into the active site cleft, then stretching through the RNA-exit channel to connect the N- and C-terminal domains. The holoenzyme structure provides insight into the structural organization of transcription intermediate complexes and into the mechanism of transcription initiation.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
ARN Polimerasas Dirigidas por ADN
/
Thermus thermophilus
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
Nature
Año:
2002
Tipo del documento:
Article
País de afiliación:
Japón