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| | <StructureSection load='1u55' size='340' side='right'caption='[[1u55]], [[Resolution|resolution]] 1.77Å' scene=''> | | <StructureSection load='1u55' size='340' side='right'caption='[[1u55]], [[Resolution|resolution]] 1.77Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1u55]] is a 2 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=1U55 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1U55 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1u55]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caldanaerobacter_subterraneus_subsp._tengcongensis Caldanaerobacter subterraneus subsp. tengcongensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U55 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U55 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.77Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1u4h|1u4h]], [[1u56|1u56]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <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=119072 AS 1.2430])</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=1u55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u55 OCA], [https://pdbe.org/1u55 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u55 RCSB], [https://www.ebi.ac.uk/pdbsum/1u55 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u55 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1u55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u55 OCA], [http://pdbe.org/1u55 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1u55 RCSB], [http://www.ebi.ac.uk/pdbsum/1u55 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1u55 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8RBX6_CALS4 Q8RBX6_CALS4] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: As 1 2430]] | + | [[Category: Caldanaerobacter subterraneus subsp. tengcongensis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Boon, E M]] | + | [[Category: Boon EM]] |
| - | [[Category: Karow, D S]] | + | [[Category: Karow DS]] |
| - | [[Category: Kuriyan, J]] | + | [[Category: Kuriyan J]] |
| - | [[Category: Marletta, M A]] | + | [[Category: Marletta MA]] |
| - | [[Category: Pellicena, P]] | + | [[Category: Pellicena P]] |
| - | [[Category: Chemotaxis]]
| + | |
| - | [[Category: H-nox domain]]
| + | |
| - | [[Category: Heme]]
| + | |
| - | [[Category: Oxygen sensor]]
| + | |
| - | [[Category: Signal transduction]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
Function
Q8RBX6_CALS4
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 PubMed
Soluble 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 Also
References
- ↑ Pellicena P, Karow DS, Boon EM, Marletta MA, Kuriyan J. Crystal structure of an oxygen-binding heme domain related to soluble guanylate cyclases. Proc Natl Acad Sci U S A. 2004 Aug 31;101(35):12854-9. Epub 2004 Aug 23. PMID:15326296 doi:10.1073/pnas.0405188101
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