2ofm

From Proteopedia

(Difference between revisions)

Revision as of 07:51, 2 March 2022

1.11 A Crystal Structure of Apo Nitrophorin 4 From Rhodnius Prolixus

Structural highlights

2ofm 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:	1x8o
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 from Rhodnius prolixus, the kissing bug, are heme-containing proteins used for the transport of nitric oxide to aide the insect in obtaining a blood meal. The Rhodnius nitrophorins display an eight-stranded antiparallel beta-barrel motif, typical of lipocalins, with a histidine-linked heme in the open end of the barrel. Heme is stabilized in the ferric state and highly distorted, displaying a ruffled conformation that may be of importance in the setting of the reduction potential. To help in understanding the means by which the protein matrix, an inherently soft material, is able to distort the heme from its low-energy planar conformation, we have determined the crystal structure of apo-nitrophorin 4-1.1 A resolution. Removal of the heme from nitrophorin 4 has very little effect on its structure: The heme binding cavity remains open and the loops near the cavity entrance respond to lower pH in the same manner as the intact protein. We conclude that the general stability of the lipocalin fold and apparent rigidity of the beta-barrel provide the means for distorting the heme cofactor.

Apo-nitrophorin 4 at atomic resolution.,Amoia AM, Montfort WR Protein Sci. 2007 Sep;16(9):2076-81. Epub 2007 Jul 27. PMID:17660249^[1]

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

References

↑ Amoia AM, Montfort WR. Apo-nitrophorin 4 at atomic resolution. Protein Sci. 2007 Sep;16(9):2076-81. Epub 2007 Jul 27. PMID:17660249 doi:10.1110/ps.072981907

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ofm"

@@ Line 3: / Line 3: @@
 <StructureSection load='2ofm' size='340' side='right'caption='[[2ofm]], [[Resolution|resolution]] 1.11&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ofm]] 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=2OFM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2OFM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2ofm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhopr Rhopr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OFM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OFM FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1x8o|1x8o]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1x8o|1x8o]]</div></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=2ofm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ofm OCA], [http://pdbe.org/2ofm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ofm RCSB], [http://www.ebi.ac.uk/pdbsum/2ofm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ofm 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=2ofm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ofm OCA], [https://pdbe.org/2ofm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ofm RCSB], [https://www.ebi.ac.uk/pdbsum/2ofm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ofm ProSAT]</span></td></tr>
 </table>
 == 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]

2ofm

From Proteopedia

Revision as of 07:51, 2 March 2022

1.11 A Crystal Structure of Apo Nitrophorin 4 From Rhodnius Prolixus

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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