7pdf: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Unreleased structure'''
-The entry 7pdf is ON HOLD  until sometime in the future
+==focus refinement of soluble domain of adenylyl cyclase 9 in complex with Gs protein alpha subunit and MANT-GTP==
+<StructureSection load='7pdf' size='340' side='right'caption='[[7pdf]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7pdf]] is a 2 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=7PDF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PDF 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]] 3.8&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=7pdf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pdf OCA], [https://pdbe.org/7pdf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pdf RCSB], [https://www.ebi.ac.uk/pdbsum/7pdf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pdf ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/E1BM79_BOVIN E1BM79_BOVIN]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Adenylyl cyclase 9 (AC9) is a membrane-bound enzyme that converts ATP into cAMP. The enzyme is weakly activated by forskolin, fully activated by the G protein Galphas subunit and is autoinhibited by the AC9 C-terminus. Although our recent structural studies of the AC9-Galphas complex provided the framework for understanding AC9 autoinhibition, the conformational changes that AC9 undergoes in response to activator binding remains poorly understood. Here, we present the cryo-EM structures of AC9 in several distinct states: (i) AC9 bound to a nucleotide inhibitor MANT-GTP, (ii) bound to an artificial activator (DARPin C4) and MANT-GTP, (iii) bound to DARPin C4 and a nucleotide analogue ATPalphaS, (iv) bound to Galphas and MANT-GTP. The artificial activator DARPin C4 partially activates AC9 by binding at a site that overlaps with the Galphas binding site. Together with the previously observed occluded and forskolin-bound conformations, structural comparisons of AC9 in the four conformations described here show that secondary structure rearrangements in the region surrounding the forskolin binding site are essential for AC9 activation.
-Authors: Qi, C., Korkhov, V.M.
+Structural basis of adenylyl cyclase 9 activation.,Qi C, Lavriha P, Mehta V, Khanppnavar B, Mohammed I, Li Y, Lazaratos M, Schaefer JV, Dreier B, Pluckthun A, Bondar AN, Dessauer CW, Korkhov VM Nat Commun. 2022 Feb 24;13(1):1045. doi: 10.1038/s41467-022-28685-y. PMID:35210418<ref>PMID:35210418</ref>
-Description: focus refinement of soluble domain of adenylyl cyclase 9 in complex with Gs protein alpha subunit and MANT-GTP
+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 7pdf" style="background-color:#fffaf0;"></div>
-[[Category: Qi, C]]
+==See Also==
+*[[3D Adenylyl cyclase 3D structures|3D Adenylyl cyclase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Bos taurus]]
+[[Category: Large Structures]]
+[[Category: Korkhov VM]]
+[[Category: Qi C]]