|
|
| (One intermediate revision not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==NMR structure of the H103G mutant SO2144 H-NOX domain from Shewanella oneidensis in the Fe(II)CO ligation state== | | ==NMR structure of the H103G mutant SO2144 H-NOX domain from Shewanella oneidensis in the Fe(II)CO ligation state== |
| - | <StructureSection load='2kil' size='340' side='right' caption='[[2kil]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2kil' size='340' side='right'caption='[[2kil]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2kil]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_700550 Atcc 700550]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KIL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KIL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2kil]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Shewanella_oneidensis Shewanella oneidensis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KIL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KIL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2kii|2kii]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SO2144, SO_2144 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=70863 ATCC 700550])</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=2kil FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kil OCA], [https://pdbe.org/2kil PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kil RCSB], [https://www.ebi.ac.uk/pdbsum/2kil PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kil ProSAT]</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=2kil FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kil OCA], [http://pdbe.org/2kil PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kil RCSB], [http://www.ebi.ac.uk/pdbsum/2kil PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2kil ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8EF49_SHEON Q8EF49_SHEON] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 32: |
Line 33: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 700550]] | + | [[Category: Large Structures]] |
| - | [[Category: Erbil, W K]] | + | [[Category: Shewanella oneidensis]] |
| - | [[Category: H-nox]] | + | [[Category: Erbil WK]] |
| - | [[Category: Unknown function]]
| + | |
| Structural highlights
Function
Q8EF49_SHEON
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
Heme nitric oxide/oxygen (H-NOX) proteins are found in eukaryotes where they are typically part of a larger protein such as soluble guanylate cyclase and in prokaryotes where they are often found in operons with a histidine kinase, suggesting that H-NOX proteins serve as sensors for NO and O(2) in signaling pathways. The Fe(II)-NO complex of the H-NOX protein from Shewanella oneidensis inhibits the autophosphorylation of the operon-associated histidine kinase, whereas the ligand-free H-NOX has no effect on the kinase. NMR spectroscopy was used to determine the structures of the Fe(II)-CO complex of the S. oneidensis H-NOX and the Fe(II)-CO complex of the H103G H-NOX mutant as a mimic of the ligand-free and kinase-inhibitory Fe(II)-NO H-NOX, respectively. The results provide a molecular glimpse into the ligand-induced conformational changes that may underlie kinase inhibition and the subsequent control of downstream signaling.
A structural basis for H-NOX signaling in Shewanella oneidensis by trapping a histidine kinase inhibitory conformation.,Erbil WK, Price MS, Wemmer DE, Marletta MA Proc Natl Acad Sci U S A. 2009 Nov 24;106(47):19753-60. Epub 2009 Nov 16. PMID:19918063[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Erbil WK, Price MS, Wemmer DE, Marletta MA. A structural basis for H-NOX signaling in Shewanella oneidensis by trapping a histidine kinase inhibitory conformation. Proc Natl Acad Sci U S A. 2009 Nov 24;106(47):19753-60. Epub 2009 Nov 16. PMID:19918063
|
