Conformational Dynamics of apo-GlnBP Revealed by Experimental and Computational Analysis.
Angew Chem Int Ed Engl
; 55(45): 13990-13994, 2016 11 02.
Article
en En
| MEDLINE
| ID: mdl-27730716
ABSTRACT
The glutamine binding protein (GlnBP) binds l-glutamine and cooperates with its cognate transporters during glutamine uptake. Crystal structure analysis has revealed an open and a closed conformation for apo- and holo-GlnBP, respectively. However, the detailed conformational dynamics have remained unclear. Herein, we combined NMR spectroscopy, MD simulations, and single-molecule FRET techniques to decipher the conformational dynamics of apo-GlnBP. The NMR residual dipolar couplings of apo-GlnBP were in good agreement with a MD-derived structure ensemble consisting of four metastable states. The open and closed conformations are the two major states. This four-state model was further validated by smFRET experiments and suggests the conformational selection mechanism in ligand recognition of GlnBP.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Proteínas Portadoras
/
Simulación de Dinámica Molecular
/
Glutamina
Idioma:
En
Revista:
Angew Chem Int Ed Engl
Año:
2016
Tipo del documento:
Article