Crystal structure of Escherichia coli sigmaE with the cytoplasmic domain of its anti-sigma RseA.
Mol Cell
; 11(4): 1067-78, 2003 Apr.
Article
en En
| MEDLINE
| ID: mdl-12718891
ABSTRACT
The sigma factors are the key regulators of bacterial transcription. ECF (extracytoplasmic function) sigma's are the largest and most divergent group of sigma(70) family members. ECF sigma's are normally sequestered in an inactive complex by their specific anti-sigma factor, which often spans the inner membrane. Here, we determined the 2 A resolution crystal structure of the Escherichia coli ECF sigma factor sigma(E) in an inhibitory complex with the cytoplasmic domain of its anti-sigma, RseA. Despite extensive sequence variability, the two major domains of sigma(E) are virtually identical in structure to the corresponding domains of other sigma(70) family members. In combination with a model of the sigma(E) holoenzyme and biochemical data, the structure reveals that RseA functions by sterically occluding the two primary binding determinants on sigma(E) for core RNA polymerase.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Factor sigma
/
Factores de Transcripción
/
Regulación Bacteriana de la Expresión Génica
/
Genes Reguladores
/
Proteínas de Escherichia coli
/
Escherichia coli
/
Proteínas de la Membrana
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
Mol Cell
Asunto de la revista:
BIOLOGIA MOLECULAR
Año:
2003
Tipo del documento:
Article
País de afiliación:
Estados Unidos