3jbq

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== Structural highlights ==
== Structural highlights ==
<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>
<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>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3jab|3jab]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 11&#8491;</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>
<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 ==
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[[https://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.
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[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]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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<ref>PMID:25809480</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3jbq" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
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[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Agosto, M A]]
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[[Category: Agosto MA]]
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[[Category: Baehr, W]]
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[[Category: Baehr W]]
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[[Category: Baker, M L]]
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[[Category: Baker ML]]
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[[Category: Constantine, R]]
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[[Category: Constantine R]]
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[[Category: He, F]]
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[[Category: He F]]
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[[Category: Schmid, M F]]
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[[Category: Schmid MF]]
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[[Category: Wensel, T G]]
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[[Category: Wensel TG]]
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[[Category: Zhang, Z]]
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[[Category: Zhang Z]]
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[[Category: Hydrolase-immune system complex]]
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[[Category: Pde6]]
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[[Category: Phosphodiesterase]]
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[[Category: Photoreceptor]]
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Revision as of 08:43, 7 February 2024

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

3jbq, resolution 11.00Å

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