An alternative flexible conformation of the E. coli HUß2 protein: structural, dynamics, and functional aspects.
Eur Biophys J
; 40(2): 117-29, 2011 Feb.
Article
em En
| MEDLINE
| ID: mdl-20936276
ABSTRACT
The histone-like HU protein is the major nucleoid-associated protein involved in the dynamics and structure of the bacterial chromosome. Under physiological conditions, the three possible dimeric forms of the E. coli HU protein (EcHUα2, EcHUß2, and EcHUαß) are in thermal equilibrium between two dimeric conformations (N2 â I2) varying in their secondary structure content. High-temperature molecular dynamics simulations combined with NMR experiments provide information about structural and dynamics features at the atomic level for the N2 to I2 thermal transition of the EcHUß2 homodimer. On the basis of these data, a realistic 3D model is proposed for the major I2 conformation of EcHUß2. This model is in agreement with previous experimental data.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Desnaturação Proteica
/
Proteínas de Bactérias
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Proteínas de Escherichia coli
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Proteínas de Ligação a DNA
/
Simulação de Dinâmica Molecular
Tipo de estudo:
Prognostic_studies
Idioma:
En
Ano de publicação:
2011
Tipo de documento:
Article