2o09: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2o09]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Nostoc_sp._pcc_7120 Nostoc sp. pcc 7120]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O09 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2O09 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2o09]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Nostoc_sp._pcc_7120 Nostoc sp. pcc 7120]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O09 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2O09 FirstGlance]. <br> | ||
</td></tr><tr><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='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><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2o0c|2o0c]], [[2o0g|2o0g]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2o0c|2o0c]], [[2o0g|2o0g]]</td></tr> | ||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">alr2278 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=103690 Nostoc sp. PCC 7120])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">alr2278 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=103690 Nostoc sp. PCC 7120])</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2o09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o09 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2o09 RCSB], [http://www.ebi.ac.uk/pdbsum/2o09 PDBsum]</span></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=2o09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o09 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2o09 RCSB], [http://www.ebi.ac.uk/pdbsum/2o09 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Nostoc sp. pcc 7120]] | [[Category: Nostoc sp. pcc 7120]] | ||
[[Category: Akker, F van den | [[Category: Akker, F van den]] | ||
[[Category: Ma, X | [[Category: Ma, X]] | ||
[[Category: Co]] | [[Category: Co]] | ||
[[Category: Guanylyl cyclase]] | [[Category: Guanylyl cyclase]] | ||
Revision as of 16:19, 19 January 2015
Crystal structure of the H-NOX domain from Nostoc sp. PCC 7120Crystal structure of the H-NOX domain from Nostoc sp. PCC 7120
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 PubMedDiatomic ligand discrimination by soluble guanylyl cyclase (sGC) is paramount to cardiovascular homeostasis and neuronal signaling. Nitric oxide (NO) stimulates sGC activity 200-fold compared with only four-fold by carbon monoxide (CO). The molecular details of ligand discrimination and differential response to NO and CO are not well understood. These ligands are sensed by the heme domain of sGC, which belongs to the heme nitric oxide oxygen (H-NOX) domain family, also evolutionarily conserved in prokaryotes. Here we report crystal structures of the free, NO-bound, and CO-bound H-NOX domains of a cyanobacterial homolog. These structures and complementary mutational analysis in sGC reveal a molecular ruler mechanism that allows sGC to favor NO over CO while excluding oxygen, concomitant to signaling that exploits differential heme pivoting and heme bending. The heme thereby serves as a flexing wedge, allowing the N-terminal subdomain of H-NOX to shift concurrent with the transition of the six- to five-coordinated NO-bound state upon sGC activation. This transition can be modulated by mutations at sGC residues 74 and 145 and corresponding residues in the cyanobacterial H-NOX homolog. NO and CO differentially activate soluble guanylyl cyclase via a heme pivot-bend mechanism.,Ma X, Sayed N, Beuve A, van den Akker F EMBO J. 2007 Jan 24;26(2):578-88. Epub 2007 Jan 11. PMID:17215864[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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