Structural highlights
Function
PDE5A_BOVIN Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-GMP (PubMed:8530505). Specifically regulates nitric-oxide-generated cGMP (By similarity).[UniProtKB:O76074][1] PDE6C_BOVIN As cone-specific cGMP phosphodiesterase, it plays an essential role in light detection and cone phototransduction by rapidly decreasing intracellular levels of cGMP.[UniProtKB:P51160]
Publication Abstract from PubMed
The cGMP phosphodiesterase of rod photoreceptor cells, PDE6, is the key effector enzyme in phototransduction. Two large catalytic subunits, PDE6alpha and -beta, each contain one catalytic domain and two non-catalytic GAF domains, whereas two small inhibitory PDE6gamma 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 approximately 11 A 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/delta) indicated the location of the PDE6 C-terminal prenylations. Reconstructions of complexes with Fab fragments bound to N or C termini of PDE6gamma revealed that PDE6gamma stretches from the catalytic domain at one end of the holoenzyme to the GAF-A domain at the other. Removal of PDE6gamma caused dramatic structural rearrangements, which were reversed upon its restoration.
Domain Organization and Conformational Plasticity of the G Protein Effector, PDE6.,Zhang Z, He F, Constantine R, Baker ML, Baehr W, Schmid MF, Wensel TG, Agosto MA J Biol Chem. 2015 May 15;290(20):12833-43. doi: 10.1074/jbc.M115.647636. Epub, 2015 Mar 25. PMID:25809480[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ McAllister-Lucas LM, Haik TL, Colbran JL, Sonnenburg WK, Seger D, Turko IV, Beavo JA, Francis SH, Corbin JD. An essential aspartic acid at each of two allosteric cGMP-binding sites of a cGMP-specific phosphodiesterase. J Biol Chem. 1995 Dec 22;270(51):30671-9. PMID:8530505 doi:10.1074/jbc.270.51.30671
- ↑ Zhang Z, He F, Constantine R, Baker ML, Baehr W, Schmid MF, Wensel TG, Agosto MA. Domain Organization and Conformational Plasticity of the G Protein Effector, PDE6. J Biol Chem. 2015 May 15;290(20):12833-43. doi: 10.1074/jbc.M115.647636. Epub, 2015 Mar 25. PMID:25809480 doi:http://dx.doi.org/10.1074/jbc.M115.647636
