Molecular function of the prolyl cis/trans isomerase and metallochaperone SlyD.
Biol Chem
; 394(8): 965-75, 2013 Aug.
Article
em En
| MEDLINE
| ID: mdl-23585180
ABSTRACT
SlyD is a bacterial two-domain protein that functions as a molecular chaperone, a prolyl cis/trans isomerase, and a nickel-binding protein. This review summarizes recent findings about the molecular enzyme mechanism of SlyD. The chaperone function located in one domain of SlyD is involved in twin-arginine translocation and increases the catalytic efficiency of the prolyl cis/trans isomerase domain in protein folding by two orders of magnitude. The C-terminal tail of SlyD binds Ni2+ ions and supplies them for the maturation of [NiFe] hydrogenases. A combined biochemical and biophysical analysis revealed the molecular basis of the delicate interplay of the different domains of SlyD for optimal function.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Bactérias
/
Proteínas de Bactérias
/
Peptidilprolil Isomerase
Idioma:
En
Ano de publicação:
2013
Tipo de documento:
Article