8hbe: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8hbe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HBE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HBE FirstGlance]. <br> | <table><tr><td colspan='2'>[[8hbe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HBE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HBE FirstGlance]. <br> | ||
</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> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.2Å</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=8hbe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hbe OCA], [https://pdbe.org/8hbe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hbe RCSB], [https://www.ebi.ac.uk/pdbsum/8hbe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hbe ProSAT]</span></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=8hbe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hbe OCA], [https://pdbe.org/8hbe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hbe RCSB], [https://www.ebi.ac.uk/pdbsum/8hbe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hbe ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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Soluble guanylate cyclase (sGC) is the primary receptor for nitric oxide (NO). The binding of NO to the haem of sGC induces a large conformational change in the enzyme and activates its cyclase activity. However, whether NO binds to the proximal site or the distal site of haem in the fully activated state remains under debate. Here, we present cryo-EM maps of sGC in the NO-activated state at high resolutions, allowing the observation of the density of NO. These cryo-EM maps show the binding of NO to the distal site of haem in the NO-activated state. | Soluble guanylate cyclase (sGC) is the primary receptor for nitric oxide (NO). The binding of NO to the haem of sGC induces a large conformational change in the enzyme and activates its cyclase activity. However, whether NO binds to the proximal site or the distal site of haem in the fully activated state remains under debate. Here, we present cryo-EM maps of sGC in the NO-activated state at high resolutions, allowing the observation of the density of NO. These cryo-EM maps show the binding of NO to the distal site of haem in the NO-activated state. | ||
NO binds to the distal site of haem in the fully activated soluble guanylate cyclase.,Liu R, Kang Y, Chen L Nitric Oxide. 2023 | NO binds to the distal site of haem in the fully activated soluble guanylate cyclase.,Liu R, Kang Y, Chen L Nitric Oxide. 2023 May 1;134-135:17-22. doi: 10.1016/j.niox.2023.03.002. Epub , 2023 Mar 25. PMID:36972843<ref>PMID:36972843</ref> | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 8hbe" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 8hbe" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Guanylate cyclase 3D structures|Guanylate cyclase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Latest revision as of 10:37, 3 July 2024
Structure of human soluble guanylate cyclase in the inactive state at 3.1 angstromStructure of human soluble guanylate cyclase in the inactive state at 3.1 angstrom
Structural highlights
DiseaseGCYA1_HUMAN Moyamoya disease with early-onset achalasia. The disease is caused by mutations affecting the gene represented in this entry. FunctionPublication Abstract from PubMedSoluble guanylate cyclase (sGC) is the primary receptor for nitric oxide (NO). The binding of NO to the haem of sGC induces a large conformational change in the enzyme and activates its cyclase activity. However, whether NO binds to the proximal site or the distal site of haem in the fully activated state remains under debate. Here, we present cryo-EM maps of sGC in the NO-activated state at high resolutions, allowing the observation of the density of NO. These cryo-EM maps show the binding of NO to the distal site of haem in the NO-activated state. NO binds to the distal site of haem in the fully activated soluble guanylate cyclase.,Liu R, Kang Y, Chen L Nitric Oxide. 2023 May 1;134-135:17-22. doi: 10.1016/j.niox.2023.03.002. Epub , 2023 Mar 25. PMID:36972843[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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