6r4o
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of a truncated adenylyl cyclase bound to MANT-GTP, forskolin and an activated stimulatory Galphas protein== | |
| + | <StructureSection load='6r4o' size='340' side='right'caption='[[6r4o]], [[Resolution|resolution]] 4.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6r4o]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6R4O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6R4O FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FOK:FORSKOLIN'>FOK</scene>, <scene name='pdbligand=GSP:5-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=ONM:3-O-(N-METHYLANTHRANILOYL)-GUANOSINE-5-TRIPHOSPHATE'>ONM</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6r4o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r4o OCA], [http://pdbe.org/6r4o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6r4o RCSB], [http://www.ebi.ac.uk/pdbsum/6r4o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6r4o ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/GNAS2_BOVIN GNAS2_BOVIN]] Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(s) protein is involved in hormonal regulation of adenylate cyclase: it activates the cyclase in response to beta-adrenergic stimuli. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Membrane-integral adenylyl cyclases (ACs) are key enzymes in mammalian heterotrimeric GTP-binding protein (G protein)-dependent signal transduction, which is important in many cellular processes. Signals received by the G protein-coupled receptors are conveyed to ACs through G proteins to modulate the levels of cellular cyclic adenosine monophosphate (cAMP). Here, we describe the cryo-electron microscopy structure of the bovine membrane AC9 bound to an activated G protein alphas subunit at 3.4-angstrom resolution. The structure reveals the organization of the membrane domain and helical domain that spans between the membrane and catalytic domains of AC9. The carboxyl-terminal extension of the catalytic domain occludes both the catalytic and the allosteric sites of AC9, inducing a conformation distinct from the substrate- and activator-bound state, suggesting a regulatory role in cAMP production. | ||
| - | + | The structure of a membrane adenylyl cyclase bound to an activated stimulatory G protein.,Qi C, Sorrentino S, Medalia O, Korkhov VM Science. 2019 Apr 26;364(6438):389-394. doi: 10.1126/science.aav0778. PMID:31023924<ref>PMID:31023924</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6r4o" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Korkhov, V M]] | ||
| + | [[Category: Medalia, O]] | ||
| + | [[Category: Qi, C]] | ||
| + | [[Category: Sorrentino, S]] | ||
| + | [[Category: Adenylyl cyclase]] | ||
| + | [[Category: Forskolin]] | ||
| + | [[Category: G protein]] | ||
| + | [[Category: Mant-gtp]] | ||
| + | [[Category: Membrane protein]] | ||
Revision as of 11:28, 10 May 2019
Structure of a truncated adenylyl cyclase bound to MANT-GTP, forskolin and an activated stimulatory Galphas protein
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