Structure of catalytically competent intein caught in a redox trap with functional and evolutionary implications.
Nat Struct Mol Biol
; 18(5): 630-3, 2011 May.
Article
em En
| MEDLINE
| ID: mdl-21460844
ABSTRACT
Here we describe self-splicing proteins, called inteins, that function as redox-responsive switches in bacteria. Redox regulation was achieved by engineering a disulfide bond between the intein's catalytic cysteine and a cysteine in the flanking 'extein' sequence. This interaction was validated by an X-ray structure, which includes a transient splice junction. A natural analog of the designed system was identified in Pyrococcus abyssi, suggesting an unprecedented form of adaptive, post-translational regulation.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
/
Evolução Molecular
/
Inteínas
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DNA Polimerase III
Idioma:
En
Ano de publicação:
2011
Tipo de documento:
Article