1d3s

From Proteopedia

(Difference between revisions)

Revision as of 08:08, 10 September 2015

1.4 A crystal structure of nitrophorin 4 from Rhodnius prolixis at pH=5.6.

Structural highlights

1d3s is a 1 chain structure with sequence from Rhopr. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1np4, 1d2u
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

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

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Weichsel A, Andersen JF, Roberts SA, Montfort WR. Nitric oxide binding to nitrophorin 4 induces complete distal pocket burial. Nat Struct Biol. 2000 Jul;7(7):551-4. PMID:10876239 doi:10.1038/76769

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1d3s"

@@ Line 5: / Line 5: @@
 </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>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1np4|1np4]], [[1d2u|1d2u]]</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=1d3s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d3s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1d3s RCSB], [http://www.ebi.ac.uk/pdbsum/1d3s 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=1d3s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d3s OCA], [http://pdbe.org/1d3s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1d3s RCSB], [http://www.ebi.ac.uk/pdbsum/1d3s PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 27: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1d3s" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

1d3s

From Proteopedia

Revision as of 08:08, 10 September 2015

1.4 A crystal structure of nitrophorin 4 from Rhodnius prolixis at pH=5.6.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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