1xbn: Difference between revisions
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==Crystal structure of a bacterial nitric oxide sensor: an ortholog of mammalian soluble guanylate cyclase heme domain== | ==Crystal structure of a bacterial nitric oxide sensor: an ortholog of mammalian soluble guanylate cyclase heme domain== | ||
<StructureSection load='1xbn' size='340' side='right' caption='[[1xbn]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1xbn' size='340' side='right'caption='[[1xbn]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1xbn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cals4 Cals4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XBN OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[1xbn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cals4 Cals4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XBN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1XBN 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>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></td></tr> | </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>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tar4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273068 CALS4])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tar4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273068 CALS4])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1xbn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xbn OCA], [http://pdbe.org/1xbn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xbn RCSB], [http://www.ebi.ac.uk/pdbsum/1xbn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xbn ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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==See Also== | ==See Also== | ||
*[[Chemotaxis protein|Chemotaxis protein]] | *[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]] | ||
*[[Methyl-accepting chemotaxis protein|Methyl-accepting chemotaxis protein]] | *[[Methyl-accepting chemotaxis protein|Methyl-accepting chemotaxis protein]] | ||
== References == | == References == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Cals4]] | [[Category: Cals4]] | ||
[[Category: Large Structures]] | |||
[[Category: Nioche, P]] | [[Category: Nioche, P]] | ||
[[Category: Raman, C S]] | [[Category: Raman, C S]] | ||
Revision as of 12:52, 6 January 2021
Crystal structure of a bacterial nitric oxide sensor: an ortholog of mammalian soluble guanylate cyclase heme domainCrystal structure of a bacterial nitric oxide sensor: an ortholog of mammalian soluble guanylate cyclase heme domain
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedNitric oxide (NO) is extremely toxic to Clostridium botulinum, but its molecular targets are unknown. Here, we identify a heme protein sensor (SONO) that displays femtomolar affinity for NO. The crystal structure of the SONO heme domain reveals a previously undescribed fold and a strategically placed tyrosine residue that modulates heme-nitrosyl coordination. Furthermore, the domain architecture of a SONO ortholog cloned from Chlamydomonas reinhardtii indicates that NO signaling through cyclic guanosine monophosphate arose before the origin of multicellular eukaryotes. Our findings have broad implications for understanding bacterial responses to NO, as well as for the activation of mammalian NO-sensitive guanylyl cyclase. Femtomolar sensitivity of a NO sensor from Clostridium botulinum.,Nioche P, Berka V, Vipond J, Minton N, Tsai AL, Raman CS Science. 2004 Nov 26;306(5701):1550-3. Epub 2004 Oct 7. PMID:15472039[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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