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6mzb
From Proteopedia
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<SX load='6mzb' size='340' side='right' viewer='molstar' caption='[[6mzb]], [[Resolution|resolution]] 3.40Å' scene=''> | <SX load='6mzb' size='340' side='right' viewer='molstar' caption='[[6mzb]], [[Resolution|resolution]] 3.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6mzb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[6mzb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MZB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MZB FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=35G:GUANOSINE-3,5-MONOPHOSPHATE'>35G</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6mzb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mzb OCA], [https://pdbe.org/6mzb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mzb RCSB], [https://www.ebi.ac.uk/pdbsum/6mzb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mzb 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=6mzb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mzb OCA], [https://pdbe.org/6mzb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mzb RCSB], [https://www.ebi.ac.uk/pdbsum/6mzb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mzb ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/PDE6B_BOVIN PDE6B_BOVIN] This protein participates in processes of transmission and amplification of the visual signal. Necessary for the formation of a functional phosphodiesterase holoenzyme. | |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Cyclic nucleotide phosphodiesterases (PDEs) work in conjunction with adenylate/guanylate cyclases to regulate the key second messengers of G protein-coupled receptor signaling. Previous attempts to determine the full-length structure of PDE family members at high-resolution have been hindered by structural flexibility, especially in their linker regions and N- and C-terminal ends. Therefore, most structure-activity relationship studies have so far focused on truncated and conserved catalytic domains rather than the regulatory domains that allosterically govern the activity of most PDEs. Here, we used single-particle cryo-electron microscopy to determine the structure of the full-length PDE6alphabeta2gamma complex. The final density map resolved at 3.4 A reveals several previously unseen structural features, including a coiled N-terminal domain and the interface of PDE6gamma subunits with the PDE6alphabeta heterodimer. Comparison of the PDE6alphabeta2gamma complex with the closed state of PDE2A sheds light on the conformational changes associated with the allosteric activation of type I PDEs. | Cyclic nucleotide phosphodiesterases (PDEs) work in conjunction with adenylate/guanylate cyclases to regulate the key second messengers of G protein-coupled receptor signaling. Previous attempts to determine the full-length structure of PDE family members at high-resolution have been hindered by structural flexibility, especially in their linker regions and N- and C-terminal ends. Therefore, most structure-activity relationship studies have so far focused on truncated and conserved catalytic domains rather than the regulatory domains that allosterically govern the activity of most PDEs. Here, we used single-particle cryo-electron microscopy to determine the structure of the full-length PDE6alphabeta2gamma complex. The final density map resolved at 3.4 A reveals several previously unseen structural features, including a coiled N-terminal domain and the interface of PDE6gamma subunits with the PDE6alphabeta heterodimer. Comparison of the PDE6alphabeta2gamma complex with the closed state of PDE2A sheds light on the conformational changes associated with the allosteric activation of type I PDEs. | ||
| - | + | , PMID:30820458<ref>PMID:30820458</ref> | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
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__TOC__ | __TOC__ | ||
</SX> | </SX> | ||
| - | [[Category: | + | [[Category: Bos taurus]] |
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Gulati | + | [[Category: Gulati S]] |
| - | [[Category: Palczewski | + | [[Category: Palczewski K]] |
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Current revision
Cryo-EM structure of phosphodiesterase 6
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