6pas
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Inactive State of Manduca sexta soluble guanylate cyclase== | |
| + | <StructureSection load='6pas' size='340' side='right'caption='[[6pas]], [[Resolution|resolution]] 5.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6pas]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PAS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PAS FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=6pas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pas OCA], [http://pdbe.org/6pas PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pas RCSB], [http://www.ebi.ac.uk/pdbsum/6pas PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pas ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Soluble guanylate cyclase (sGC) is the primary receptor for nitric oxide (NO) in mammalian nitric oxide signaling. We determined structures of full-length Manduca sexta sGC in both inactive and active states using cryo-electron microscopy. NO and the sGC-specific stimulator YC-1 induce a 71 degrees rotation of the heme-binding beta H-NOX and PAS domains. Repositioning of the beta H-NOX domain leads to a straightening of the coiled-coil domains, which, in turn, use the motion to move the catalytic domains into an active conformation. YC-1 binds directly between the beta H-NOX domain and the two CC domains. The structural elongation of the particle observed in cryo-EM was corroborated in solution using small angle X-ray scattering (SAXS). These structures delineate the endpoints of the allosteric transition responsible for the major cyclic GMP-dependent physiological effects of NO. | ||
| - | + | Allosteric activation of the nitric oxide receptor soluble guanylate cyclase mapped by cryo-electron microscopy.,Horst BG, Yokom AL, Rosenberg DJ, Morris KL, Hammel M, Hurley JH, Marletta MA Elife. 2019 Sep 30;8. pii: 50634. doi: 10.7554/eLife.50634. PMID:31566566<ref>PMID:31566566</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6pas" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Horst, B G]] | ||
| + | [[Category: Hurley, J H]] | ||
| + | [[Category: Marletta, M A]] | ||
| + | [[Category: Yokom, A L]] | ||
| + | [[Category: Cyclase]] | ||
| + | [[Category: H-nox]] | ||
| + | [[Category: Nitric oxide]] | ||
| + | [[Category: Signaling protein]] | ||
Revision as of 06:57, 23 October 2019
Inactive State of Manduca sexta soluble guanylate cyclase
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