Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylase.
Nat Struct Biol
; 8(5): 423-6, 2001 May.
Article
em En
| MEDLINE
| ID: mdl-11323717
ABSTRACT
Regulation of protein function, often achieved by allosteric mechanisms, is central to normal physiology and cellular processes. Although numerous models have been proposed to account for the cooperative binding of ligands to allosteric proteins and enzymes, direct structural support has been lacking. Here, we used a combination of X-ray crystallography and small angle X-ray scattering in solution to provide direct structural evidence that the binding of ligand to just one of the six active sites of Escherichia coli aspartate transcarbamoylase induces a concerted structural transition from the T to the R state.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Aspartato Carbamoiltransferase
/
Escherichia coli
Idioma:
En
Revista:
Nat Struct Biol
Assunto da revista:
BIOLOGIA MOLECULAR
Ano de publicação:
2001
Tipo de documento:
Article
País de afiliação:
Estados Unidos