3jab: Difference between revisions
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New page: '''Unreleased structure''' The entry 3jab is ON HOLD Authors: Zhang, Z., He, F., Constantine, R., Baker, M.L., Baehr, W., Schmid, M.F., Wensel, T.G., Agosto, M.A. Description: Domain o... |
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The | ==Domain organization and conformational plasticity of the G protein effector, PDE6== | ||
<SX load='3jab' size='340' side='right' viewer='molstar' caption='[[3jab]], [[Resolution|resolution]] 11.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3jab]] 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=3JAB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JAB FirstGlance]. <br> | |||
</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IBM:3-ISOBUTYL-1-METHYLXANTHINE'>IBM</scene></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=3jab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jab OCA], [https://pdbe.org/3jab PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jab RCSB], [https://www.ebi.ac.uk/pdbsum/3jab PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jab ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0M3KKT0_BOVIN A0A0M3KKT0_BOVIN] | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:25809480</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 3jab" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: Baker | __TOC__ | ||
[[Category: | </SX> | ||
[[Category: | [[Category: Bos taurus]] | ||
[[Category: Schmid | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: Agosto MA]] | |||
[[Category: Baehr W]] | |||
[[Category: Baker ML]] | |||
[[Category: Constantine R]] | |||
[[Category: He F]] | |||
[[Category: Schmid MF]] | |||
[[Category: Wensel TG]] | |||
[[Category: Zhang Z]] | |||
Latest revision as of 05:55, 17 October 2024
Domain organization and conformational plasticity of the G protein effector, PDE6
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