3JBQ

Domain Organization and Conformational Plasticity of the G Protein Effector, PDE6

Summary for 3JBQ

• Entry DOI: 10.2210/pdb3jbq/pdb
• Related: 3JAB
• EMDB information: 6258
• Descriptor: IgG1-kappa 2E8 light chain, IgG1-kappa 2E8 heavy chain, phosphodiesterase 5/6 chimera catalytic domain, ... (6 entities in total)
• Functional Keywords: phosphodiesterase, photoreceptor, pde6, hydrolase-immune system complex, hydrolase/immune system
• Biological source: Mus musculus (mouse); More
• Total number of polymer chains: 12
• Total formula weight: 260032.48

Authors

Zhang, Z.,He, F.,Constantine, R.,Baker, M.L.,Baehr, W.,Schmid, M.F.,Wensel, T.G.,Agosto, M.A. (deposition date: 2015-09-17, release date: 2015-09-30, Last modification date: 2024-10-16)

Primary citation

Zhang, Z.,He, F.,Constantine, R.,Baker, M.L.,Baehr, W.,Schmid, M.F.,Wensel, T.G.,Agosto, M.A.
Domain Organization and Conformational Plasticity of the G Protein Effector, PDE6.
J.Biol.Chem., 290:12833-12843, 2015

PubMed Abstract: The cGMP phosphodiesterase of rod photoreceptor cells, PDE6, is the key effector enzyme in phototransduction. Two large catalytic subunits, PDE6α and -β, 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 ∼11 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.

PubMed: 25809480
DOI: 10.1074/jbc.M115.647636

Experimental method

ELECTRON MICROSCOPY (11 Å)