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6ocv

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Current revision (07:36, 1 May 2024) (edit) (undo)
 
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==Solution structure of the H-NOX protein from Shewanella woodyi in the Fe(II)CO ligation state==
==Solution structure of the H-NOX protein from Shewanella woodyi in the Fe(II)CO ligation state==
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<StructureSection load='6ocv' size='340' side='right'caption='[[6ocv]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='6ocv' size='340' side='right'caption='[[6ocv]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6ocv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_51908 Atcc 51908]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OCV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OCV FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6ocv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Shewanella_woodyi Shewanella woodyi]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OCV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OCV FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <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=6ocv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ocv OCA], [https://pdbe.org/6ocv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ocv RCSB], [https://www.ebi.ac.uk/pdbsum/6ocv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ocv 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=6ocv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ocv OCA], [https://pdbe.org/6ocv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ocv RCSB], [https://www.ebi.ac.uk/pdbsum/6ocv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ocv ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/B1KIH6_SHEWM B1KIH6_SHEWM]
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Heme-nitric oxide/oxygen binding (H-NOX) domains bind gaseous ligands for signal transduction in organisms spanning prokaryotic and eukaryotic kingdoms. In the bioluminescent marine bacterium Shewanella woodyi (Sw), H-NOX proteins regulate quorum sensing and biofilm formation. In higher animals, soluble guanylyl cyclase (sGC) binds nitric oxide with an H-NOX domain to induce cyclase activity and regulate vascular tone, wound healing and memory formation. sGC also binds stimulator compounds targeting cardiovascular disease. The molecular details of stimulator binding to sGC remain obscure but involve a binding pocket near an interface between H-NOX and coiled-coil domains. Here, we report the full NMR structure for CO-ligated Sw H-NOX in the presence and absence of stimulator compound IWP-051, and its backbone dynamics. Non-planar heme geometry was retained using a semi-empirical quantum potential energy approach. Although IWP-051 binding is weak, a single binding conformation was found at the interface of the two H-NOX subdomains, near but not overlapping with sites identified in sGC. Binding leads to rotation of the subdomains and closure of the binding pocket. Backbone dynamics are similar across both domains except for two helix-connecting loops, which display increased dynamics that are further enhanced by compound binding. Structure-based sequence analyses indicate high sequence diversity in the binding pocket, but the pocket itself appears conserved among H-NOX proteins. The largest dynamical loop lies at the interface between Sw H-NOX and its binding partner as well as in the interface with the coiled coil in sGC, suggesting a critical role for the loop in signal transduction.
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Solution structures of the Shewanella woodyi H-NOX protein in the presence and absence of soluble guanylyl cyclase stimulator IWP-051.,Chen CY, Lee W, Renhowe PA, Jung J, Montfort WR Protein Sci. 2020 Nov 25. doi: 10.1002/pro.4005. PMID:33236796<ref>PMID:33236796</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6ocv" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 51908]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chen, C Y]]
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[[Category: Shewanella woodyi]]
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[[Category: Lee, W]]
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[[Category: Chen CY]]
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[[Category: Montfort, W R]]
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[[Category: Lee W]]
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[[Category: Hemoprotein]]
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[[Category: Montfort WR]]
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[[Category: Nitric oxide]]
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[[Category: Signaling]]
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[[Category: Signaling protein]]
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Current revision

Solution structure of the H-NOX protein from Shewanella woodyi in the Fe(II)CO ligation state

PDB ID 6ocv

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