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6r4p

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m (Protected "6r4p" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 6r4p is ON HOLD
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==Structure of a soluble domain of adenylyl cyclase bound to an activated stimulatory G protein==
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<StructureSection load='6r4p' size='340' side='right'caption='[[6r4p]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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</table>
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== Function ==
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[[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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Korkhov, V.M., Qi, C.
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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>
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Description: Structure of a soluble domain of adenylyl cyclase bound to an activated stimulatory G protein
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Korkhov, V.M]]
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<div class="pdbe-citations 6r4p" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Korkhov, V M]]
[[Category: Qi, C]]
[[Category: Qi, C]]
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[[Category: Adenylyl cyclase]]
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[[Category: G protein]]
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[[Category: Membrane protein]]
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[[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

PDB ID 6r4p

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