Domain organization and conformational plasticity of the G protein effector, PDE6.
J Biol Chem
; 290(20): 12833-43, 2015 May 15.
Article
en En
| MEDLINE
| ID: mdl-25809480
ABSTRACT
The cGMP phosphodiesterase of rod photoreceptor cells, PDE6, is the key effector enzyme in phototransduction. Two large catalytic subunits, PDE6α and -ß, each contain one catalytic domain and two non-catalytic GAF domains, whereas two small inhibitory PDE6γ subunits allow tight regulation by the G protein transducin. The structure of holo-PDE6 in complex with the ROS-1 antibody Fab fragment was determined by cryo-electron microscopy. The â¼11 Å map revealed previously unseen features of PDE6, and each domain was readily fit with high resolution structures. A structure of PDE6 in complex with prenyl-binding protein (PrBP/δ) indicated the location of the PDE6 C-terminal prenylations. Reconstructions of complexes with Fab fragments bound to N or C termini of PDE6γ revealed that PDE6γ stretches from the catalytic domain at one end of the holoenzyme to the GAF-A domain at the other. Removal of PDE6γ caused dramatic structural rearrangements, which were reversed upon its restoration.
Palabras clave
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Fragmentos Fab de Inmunoglobulinas
/
Fosfodiesterasas de Nucleótidos Cíclicos Tipo 6
/
Anticuerpos Monoclonales de Origen Murino
Límite:
Animals
/
Humans
Idioma:
En
Año:
2015
Tipo del documento:
Article