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| | <SX load='3jbq' size='340' side='right' viewer='molstar' caption='[[3jbq]], [[Resolution|resolution]] 11.00Å' scene=''> | | <SX load='3jbq' size='340' side='right' viewer='molstar' caption='[[3jbq]], [[Resolution|resolution]] 11.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3jbq]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JBQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3JBQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3jbq]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JBQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JBQ FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3jab|3jab]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 11Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3jbq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jbq OCA], [http://pdbe.org/3jbq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3jbq RCSB], [http://www.ebi.ac.uk/pdbsum/3jbq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3jbq ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3jbq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jbq OCA], [https://pdbe.org/3jbq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jbq RCSB], [https://www.ebi.ac.uk/pdbsum/3jbq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jbq ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CNRG_BOVIN CNRG_BOVIN]] Participates in processes of transmission and amplification of the visual signal. cGMP-PDEs are the effector molecules in G-protein-mediated phototransduction in vertebrate rods and cones. | + | [https://www.uniprot.org/uniprot/PDE5A_BOVIN 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]<ref>PMID:8530505</ref> [https://www.uniprot.org/uniprot/PDE6C_BOVIN 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] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Mus musculus]] | | [[Category: Mus musculus]] |
| - | [[Category: Agosto, M A]] | + | [[Category: Agosto MA]] |
| - | [[Category: Baehr, W]] | + | [[Category: Baehr W]] |
| - | [[Category: Baker, M L]] | + | [[Category: Baker ML]] |
| - | [[Category: Constantine, R]] | + | [[Category: Constantine R]] |
| - | [[Category: He, F]] | + | [[Category: He F]] |
| - | [[Category: Schmid, M F]] | + | [[Category: Schmid MF]] |
| - | [[Category: Wensel, T G]] | + | [[Category: Wensel TG]] |
| - | [[Category: Zhang, Z]] | + | [[Category: Zhang Z]] |
| - | [[Category: Hydrolase-immune system complex]]
| + | |
| - | [[Category: Pde6]]
| + | |
| - | [[Category: Phosphodiesterase]]
| + | |
| - | [[Category: Photoreceptor]]
| + | |
| 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
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