3lai: Difference between revisions
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==Structural insights into the molecular mechanism of H-NOX activation== | ==Structural insights into the molecular mechanism of H-NOX activation== | ||
<StructureSection load='3lai' size='340' side='right' caption='[[3lai]], [[Resolution|resolution]] 2.14Å' scene=''> | <StructureSection load='3lai' size='340' side='right' caption='[[3lai]], [[Resolution|resolution]] 2.14Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3lai]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3lai]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/As_1.2430 As 1.2430]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LAI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LAI 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=IMD:IMIDAZOLE'>IMD</scene></td></tr> | </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=IMD:IMIDAZOLE'>IMD</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1u55|1u55]], [[1u56|1u56]], [[1u4h|1u4h]], [[3eee|3eee]], [[3iqb|3iqb]], [[3lah|3lah]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1u55|1u55]], [[1u56|1u56]], [[1u4h|1u4h]], [[3eee|3eee]], [[3iqb|3iqb]], [[3lah|3lah]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tar4, TTE0680 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=119072 | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tar4, TTE0680 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=119072 AS 1.2430])</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=3lai FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lai OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lai RCSB], [http://www.ebi.ac.uk/pdbsum/3lai 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=3lai FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lai OCA], [http://pdbe.org/3lai PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lai RCSB], [http://www.ebi.ac.uk/pdbsum/3lai PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lai ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3lai ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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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 3lai" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: As 1 2430]] | ||
[[Category: Jr, C Olea]] | [[Category: Jr, C Olea]] | ||
[[Category: Jr, M A.Herzik]] | [[Category: Jr, M A.Herzik]] | ||
Revision as of 23:02, 4 August 2016
Structural insights into the molecular mechanism of H-NOX activationStructural insights into the molecular mechanism of H-NOX activation
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) signaling in mammals controls important processes such as smooth muscle relaxation and neurotransmission by activation of soluble guanylate cyclase (sGC). NO binding to the heme domain of sGC leads to dissociation of the iron-histidine (Fe-His) bond, which is required for enzyme activity. The heme domain of sGC belongs to a larger class of proteins called H-NOX (Heme Nitric oxide/OXygen) domains. Previous crystallographic studies on H-NOX domains demonstrate a correlation between heme bending and protein conformation. It was unclear, however, whether these structural changes were important for signal transduction. Subsequent NMR solution structures of H-NOX proteins show a conformational change, upon disconnection of the heme and proximal helix, similar to those observed in the crystallographic studies. The atomic details of these conformational changes, however, are lacking in the NMR structures especially at the heme pocket. Here, a high-resolution crystal structure of an H-NOX mutant mimicking a broken Fe-His bond is reported. This mutant exhibits specific changes in heme conformation and major N-terminal displacements relative to the wild-type H-NOX protein. Fe-His ligation is ubiquitous in all H-NOX domains, and therefore, the heme and protein conformational changes observed in the present study are likely to occur throughout the H-NOX family when NO binding leads to rupture of the Fe-His bond. Structural insights into the molecular mechanism of H-NOX activation.,Olea C Jr, Herzik MA Jr, Kuriyan J, Marletta MA Protein Sci. 2010 Feb 16. PMID:20162612[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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