7pd4: Difference between revisions

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 <StructureSection load='7pd4' size='340' side='right'caption='[[7pd4]], [[Resolution|resolution]] 4.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[7pd4]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PD4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PD4 FirstGlance]. <br>
+<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PD4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PD4 FirstGlance]. <br>
-</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=7pd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pd4 OCA], [https://pdbe.org/7pd4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pd4 RCSB], [https://www.ebi.ac.uk/pdbsum/7pd4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pd4 ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.9&#8491;</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=7pd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pd4 OCA], [https://pdbe.org/7pd4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pd4 RCSB], [https://www.ebi.ac.uk/pdbsum/7pd4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pd4 ProSAT]</span></td></tr>
 </table>
-<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.
-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>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 7pd4" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Korkhov, V M]]
+[[Category: Korkhov VM]]
-[[Category: Qi, C]]
+[[Category: Qi C]]
-[[Category: Adenylyl cyclase]]
-[[Category: Membrane protein]]
-[[Category: Signaling protein]]
-[[Category: Signalling transduction]]