Crystal structure of a SIR2 homolog-NAD complex.
Cell
; 105(2): 269-79, 2001 Apr 20.
Article
em En
| MEDLINE
| ID: mdl-11336676
ABSTRACT
The SIR2 protein family comprises a novel class of nicotinamide-adenine dinucleotide (NAD)-dependent protein deacetylases that function in transcriptional silencing, DNA repair, and life-span extension in Saccharomyces cerevisiae. Two crystal structures of a SIR2 homolog from Archaeoglobus fulgidus complexed with NAD have been determined at 2.1 A and 2.4 A resolutions. The structures reveal that the protein consists of a large domain having a Rossmann fold and a small domain containing a three-stranded zinc ribbon motif. NAD is bound in a pocket between the two domains. A distinct mode of NAD binding and an unusual configuration of the zinc ribbon motif are observed. The structures also provide important insights into the catalytic mechanism of NAD-dependent protein deacetylation by this family of enzymes.
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Bases de dados:
MEDLINE
Assunto principal:
Transativadores
/
Estrutura Terciária de Proteína
/
Archaeoglobus fulgidus
/
Proteínas Arqueais
/
Proteínas Reguladoras de Informação Silenciosa de Saccharomyces cerevisiae
/
Histona Desacetilases
/
NAD
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
Cell
Ano de publicação:
2001
Tipo de documento:
Article
País de afiliação:
Estados Unidos