View source for 6pas


==Inactive State of Manduca sexta soluble guanylate cyclase==
<SX load='6pas' size='340' side='right' viewer='molstar' caption='[[6pas]], [[Resolution|resolution]] 5.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6pas]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Manduca_sexta Manduca sexta]. 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 [https://proteopedia.org/fgij/fg.htm?mol=6PAS 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]] 5.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=6pas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pas OCA], [https://pdbe.org/6pas PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pas RCSB], [https://www.ebi.ac.uk/pdbsum/6pas PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pas ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O77105_MANSE O77105_MANSE] 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6pas" style="background-color:#fffaf0;"></div>

==See Also==
*[[Guanylate cyclase 3D structures|Guanylate cyclase 3D structures]]
== References ==
<references/>
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</SX>
[[Category: Large Structures]]
[[Category: Manduca sexta]]
[[Category: Horst BG]]
[[Category: Hurley JH]]
[[Category: Marletta MA]]
[[Category: Yokom AL]]