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| | ==1.08 A Structure of Ferrous NP4 (aquo complex)== | | ==1.08 A Structure of Ferrous NP4 (aquo complex)== |
| - | <StructureSection load='1ywd' size='340' side='right' caption='[[1ywd]], [[Resolution|resolution]] 1.08Å' scene=''> | + | <StructureSection load='1ywd' size='340' side='right'caption='[[1ywd]], [[Resolution|resolution]] 1.08Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ywd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhopr Rhopr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YWD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YWD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ywd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodnius_prolixus Rhodnius prolixus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YWD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YWD 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></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]] 1.08Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ywa|1ywa]], [[1ywb|1ywb]], [[1ywc|1ywc]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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=1ywd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ywd OCA], [http://pdbe.org/1ywd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ywd RCSB], [http://www.ebi.ac.uk/pdbsum/1ywd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ywd ProSAT]</span></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=1ywd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ywd OCA], [https://pdbe.org/1ywd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ywd RCSB], [https://www.ebi.ac.uk/pdbsum/1ywd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ywd ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NP4_RHOPR NP4_RHOPR]] Heme-based protein that deliver nitric oxide gas (NO) to the victim while feeding, resulting in vasodilation and inhibition of platelet aggregation. Also bind tightly to histamine, which is released by the host to induce wound healing (By similarity). | + | [https://www.uniprot.org/uniprot/NP4_RHOPR NP4_RHOPR] Heme-based protein that deliver nitric oxide gas (NO) to the victim while feeding, resulting in vasodilation and inhibition of platelet aggregation. Also bind tightly to histamine, which is released by the host to induce wound healing (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yw/1ywd_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yw/1ywd_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Rhopr]] | + | [[Category: Large Structures]] |
| - | [[Category: Maes, E M]] | + | [[Category: Rhodnius prolixus]] |
| - | [[Category: Montfort, W R]] | + | [[Category: Maes EM]] |
| - | [[Category: Roberts, S A]] | + | [[Category: Montfort WR]] |
| - | [[Category: Weichsel, A]] | + | [[Category: Roberts SA]] |
| - | [[Category: Beta barrel]] | + | [[Category: Weichsel A]] |
| - | [[Category: Blood clotting]]
| + | |
| - | [[Category: Ferrous heme]]
| + | |
| - | [[Category: Ligand binding protein]]
| + | |
| - | [[Category: Lipocalin fold]]
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| Structural highlights
Function
NP4_RHOPR Heme-based protein that deliver nitric oxide gas (NO) to the victim while feeding, resulting in vasodilation and inhibition of platelet aggregation. Also bind tightly to histamine, which is released by the host to induce wound healing (By similarity).
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
Nitrophorin 4 (NP4), a nitric oxide (NO)-transport protein from the blood-sucking insect Rhodnius prolixus, uses a ferric (Fe3+) heme to deliver NO to its victims. NO binding to NP4 induces a large conformational change and complete desolvation of the distal pocket. The heme is markedly nonplanar, displaying a ruffling distortion postulated to contribute to stabilization of the ferric iron. Here, we report the ferrous (Fe2+) complexes of NP4 with NO, CO, and H2O formed after chemical reduction of the protein and the characterization of these complexes by absorption spectroscopy, flash photolysis, and ultrahigh-resolution crystallography (resolutions vary from 0.9 to 1.08 A). The absorption spectra, both in solution and in the crystal, are typical for six-coordinated ferrous complexes. Closure and desolvation of the distal pocket occurs upon binding CO or NO to the iron regardless of the heme oxidation state, confirming that the conformational change is driven by distal ligand polarity. The degree of heme ruffling is coupled to the nature of the ligand and the iron oxidation state in the following order: (Fe3+)-NO > (Fe2+)-NO > (Fe2+)-CO > (Fe3+)-H2O > (Fe2+)-H2O. The ferrous coordination geometry is as expected, except for the proximal histidine bond, which is shorter than typically found in model compounds. These data are consistent with heme ruffling and coordination geometry serving to stabilize the ferric state of the nitrophorins, a requirement for their physiological function. Possible roles for heme distortion and NO bending in heme protein function are discussed.
Ultrahigh resolution structures of nitrophorin 4: heme distortion in ferrous CO and NO complexes.,Maes EM, Roberts SA, Weichsel A, Montfort WR Biochemistry. 2005 Sep 27;44(38):12690-9. PMID:16171383[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Maes EM, Roberts SA, Weichsel A, Montfort WR. Ultrahigh resolution structures of nitrophorin 4: heme distortion in ferrous CO and NO complexes. Biochemistry. 2005 Sep 27;44(38):12690-9. PMID:16171383 doi:http://dx.doi.org/10.1021/bi0506573
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