Calmodulin-induced structural changes in endothelial nitric oxide synthase.
FEBS Lett
; 587(3): 297-301, 2013 Jan 31.
Article
em En
| MEDLINE
| ID: mdl-23266515
ABSTRACT
We have derived structures of intact calmodulin (CaM)-free and CaM-bound endothelial nitric oxide synthase (eNOS) by reconstruction from cryo-electron micrographs. The CaM-free reconstruction is well fitted by the oxygenase domain dimer, but the reductase domains are not visible, suggesting they are mobile and thus delocalized. Additional protein is visible in the CaM-bound reconstruction, concentrated in volumes near two basic patches on each oxygenase domain. One of these corresponds with a presumptive docking site for the reductase domain FMN-binding module. The other is proposed to correspond with a docking site for CaM. A model is suggested in which CaM binding and docking position the reductase domains near the oxygenase domains and promote docking of the FMN-binding modules required for electron transfer.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Calmodulina
/
Óxido Nítrico Sintase Tipo III
Tipo de estudo:
Prognostic_studies
Limite:
Animals
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
2013
Tipo de documento:
Article
País de afiliação:
Estados Unidos