6r4p: Difference between revisions

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'''Unreleased structure'''


The entry 6r4p is ON HOLD
==Structure of a soluble domain of adenylyl cyclase bound to an activated stimulatory G protein==
<StructureSection load='6r4p' size='340' side='right'caption='[[6r4p]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6r4p]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6R4P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6R4P FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GSP:5-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=6r4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r4p OCA], [http://pdbe.org/6r4p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6r4p RCSB], [http://www.ebi.ac.uk/pdbsum/6r4p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6r4p 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.


Authors: Korkhov, V.M., Qi, C.
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>


Description: Structure of a soluble domain of adenylyl cyclase bound to an activated stimulatory G protein
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Korkhov, V.M]]
<div class="pdbe-citations 6r4p" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Korkhov, V M]]
[[Category: Qi, C]]
[[Category: Qi, C]]
[[Category: Adenylyl cyclase]]
[[Category: G protein]]
[[Category: Membrane protein]]
[[Category: Occluded state]]

Revision as of 11:28, 10 May 2019

Structure of a soluble domain of adenylyl cyclase bound to an activated stimulatory G protein

6r4p, resolution 3.10Å

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