Hot spots for allosteric regulation on protein surfaces.
Cell
; 147(7): 1564-75, 2011 Dec 23.
Article
em En
| MEDLINE
| ID: mdl-22196731
ABSTRACT
Recent work indicates a general architecture for proteins in which sparse networks of physically contiguous and coevolving amino acids underlie basic aspects of structure and function. These networks, termed sectors, are spatially organized such that active sites are linked to many surface sites distributed throughout the structure. Using the metabolic enzyme dihydrofolate reductase as a model system, we show that (1) the sector is strongly correlated to a network of residues undergoing millisecond conformational fluctuations associated with enzyme catalysis, and (2) sector-connected surface sites are statistically preferred locations for the emergence of allosteric control in vivo. Thus, sectors represent an evolutionarily conserved "wiring" mechanism that can enable perturbations at specific surface positions to rapidly initiate conformational control over protein function. These findings suggest that sectors enable the evolution of intermolecular communication and regulation.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas
/
Modelos Moleculares
/
Regulação Alostérica
/
Escherichia coli
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
Cell
Ano de publicação:
2011
Tipo de documento:
Article
País de afiliação:
Estados Unidos