1u4h: Difference between revisions
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==Crystal structure of an oxygen binding H-NOX domain related to soluble guanylate cyclases (oxygen complex)== | ==Crystal structure of an oxygen binding H-NOX domain related to soluble guanylate cyclases (oxygen complex)== | ||
<StructureSection load='1u4h' size='340' side='right' caption='[[1u4h]], [[Resolution|resolution]] 2.07Å' scene=''> | <StructureSection load='1u4h' size='340' side='right' caption='[[1u4h]], [[Resolution|resolution]] 2.07Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1u55|1u55]], [[1u56|1u56]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1u55|1u55]], [[1u56|1u56]]</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=119072 AS 1.2430])</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=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=1u4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u4h OCA], [http://pdbe.org/1u4h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1u4h RCSB], [http://www.ebi.ac.uk/pdbsum/1u4h 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=1u4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u4h OCA], [http://pdbe.org/1u4h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1u4h RCSB], [http://www.ebi.ac.uk/pdbsum/1u4h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1u4h ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/u4/1u4h_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/u4/1u4h_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 11:32, 21 March 2018
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 PubMedSoluble guanylate cyclases are nitric oxide-responsive signaling proteins in which the nitric oxide sensor is a heme-binding domain of unknown structure that we have termed the heme-NO and oxygen binding (H-NOX) domain. H-NOX domains are also found in bacteria, either as isolated domains, or are fused through a membrane-spanning region to methyl-accepting chemotaxis proteins. We have determined the crystal structure of an oxygen-binding H-NOX domain of one such signaling protein from the obligate anaerobe Thermoanaerobacter tengcongensis at 1.77-angstroms resolution, revealing a protein fold unrelated to known structures. Particularly striking is the structure of the protoporphyrin IX group, which is distorted from planarity to an extent not seen before in protein-bound heme groups. Comparison of the structure of the H-NOX domain in two different crystal forms suggests a mechanism whereby alteration in the degree of distortion of the heme group is coupled to changes on the molecular surface of the H-NOX domain and potentially to changes in intermolecular interactions. Crystal structure of an oxygen-binding heme domain related to soluble guanylate cyclases.,Pellicena P, Karow DS, Boon EM, Marletta MA, Kuriyan J Proc Natl Acad Sci U S A. 2004 Aug 31;101(35):12854-9. Epub 2004 Aug 23. PMID:15326296[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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