1d3s
From Proteopedia
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<StructureSection load='1d3s' size='340' side='right'caption='[[1d3s]], [[Resolution|resolution]] 1.40Å' scene=''> | <StructureSection load='1d3s' size='340' side='right'caption='[[1d3s]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1d3s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1d3s]] 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=1D3S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D3S FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</td></tr> |
| - | <tr id=' | + | <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'>[https://proteopedia.org/fgij/fg.htm?mol=1d3s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d3s OCA], [https://pdbe.org/1d3s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d3s RCSB], [https://www.ebi.ac.uk/pdbsum/1d3s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d3s 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=1d3s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d3s OCA], [https://pdbe.org/1d3s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d3s RCSB], [https://www.ebi.ac.uk/pdbsum/1d3s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d3s ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [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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</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=1d3s ConSurf]. | </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=1d3s ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The nitrophorins comprise an unusual family of proteins that use ferric (Fe(III)) heme to transport highly reactive nitric oxide (NO) from the salivary gland of a blood sucking bug to the victim, resulting in vasodilation and reduced blood coagulation. We have determined structures of nitrophorin 4 in complexes with H2O, cyanide and nitric oxide. These structures reveal a remarkable feature: the nitrophorins have a broadly open distal pocket in the absence of NO, but upon NO binding, three or more water molecules are expelled and two loops fold into the distal pocket, resulting in the packing of hydrophobic groups around the NO molecule and increased distortion of the heme. In this way, the protein apparently forms a 'hydrophobic trap' for the NO molecule. The structures are very accurate, ranging between 1.6 and 1.4 A resolutions. | ||
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| - | Nitric oxide binding to nitrophorin 4 induces complete distal pocket burial.,Weichsel A, Andersen JF, Roberts SA, Montfort WR Nat Struct Biol. 2000 Jul;7(7):551-4. PMID:10876239<ref>PMID:10876239</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1d3s" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Nitrophorin|Nitrophorin]] | *[[Nitrophorin|Nitrophorin]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Rhodnius prolixus]] |
| - | [[Category: Andersen | + | [[Category: Andersen JF]] |
| - | [[Category: Montfort | + | [[Category: Montfort WR]] |
| - | [[Category: Roberts | + | [[Category: Roberts SA]] |
| - | [[Category: Weichsel | + | [[Category: Weichsel A]] |
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Revision as of 15:45, 13 March 2024
1.4 A crystal structure of nitrophorin 4 from Rhodnius prolixis at pH=5.6.
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