6pas: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 6pas is ~~ON HOLD until Paper~~ Publication

==Inactive State of Manduca sexta soluble guanylate cyclase==

== 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>

== 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.

~~Authors~~:

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>

~~Description~~:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased~~ Structures]]

</div>

== 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]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6pas is ON HOLD  until Paper Publication
+==Inactive State of Manduca sexta soluble guanylate cyclase==
+<StructureSection load='6pas' size='340' side='right'caption='[[6pas]], [[Resolution|resolution]] 5.10&Aring;' 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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</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]]