1y21

From Proteopedia

(Difference between revisions)

Current revision

Crystal Structure of Cimex Nitrophorin NO Complex

Structural highlights

1y21 is a 1 chain structure with sequence from Cimex lectularius. This structure supersedes the now removed PDB entry 1nzh. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.75Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NP_CIMLE Heme-based protein that delivers nitric oxide gas (NO) to the victim while feeding, resulting in vasodilation (Probable). In place of heme, the heme-binding cysteine can also reversibly bind NO when it is present in high concentrations (PubMed:15637157).^[1]

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

Certain bloodsucking insects deliver nitric oxide (NO) while feeding, to induce vasodilation and inhibit blood coagulation. We have expressed, characterized, and determined the crystal structure of the Cimex lectularius (bedbug) nitrophorin, the protein responsible for NO storage and delivery, to understand how the insect successfully handles this reactive molecule. Surprisingly, NO binds not only to the ferric nitrophorin heme, but it can also be stored as an S-nitroso (SNO) conjugate of the proximal heme cysteine (Cys-60) when present at higher concentrations. EPR- and UV-visible spectroscopies, and a crystallographic structure determination to 1.75-A resolution, reveal SNO formation to proceed with reduction of the heme iron, yielding an Fe-NO complex. Stopped-flow kinetic measurements indicate that an ordered reaction mechanism takes place: initial NO binding occurs at the ferric heme and is followed by heme reduction, Cys-60 release from the heme iron, and SNO formation. Release of NO occurs through a reversal of these steps. These data provide, to our knowledge, the first view of reversible metal-assisted SNO formation in a protein and suggest a mechanism for its role in NO release from ferrous heme. This mechanism and Cimex nitrophorin structure are completely unlike those of the nitrophorins from Rhodnius prolixus, where NO protection is provided by a large conformational change that buries the heme nitrosyl complex, highlighting the remarkable evolution of proteins that assist insects in bloodfeeding.

Heme-assisted S-nitrosation of a proximal thiolate in a nitric oxide transport protein.,Weichsel A, Maes EM, Andersen JF, Valenzuela JG, Shokhireva TKh, Walker FA, Montfort WR Proc Natl Acad Sci U S A. 2005 Jan 18;102(3):594-9. Epub 2005 Jan 6. PMID:15637157^[2]

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

References

↑ Weichsel A, Maes EM, Andersen JF, Valenzuela JG, Shokhireva TKh, Walker FA, Montfort WR. Heme-assisted S-nitrosation of a proximal thiolate in a nitric oxide transport protein. Proc Natl Acad Sci U S A. 2005 Jan 18;102(3):594-9. Epub 2005 Jan 6. PMID:15637157
↑ Weichsel A, Maes EM, Andersen JF, Valenzuela JG, Shokhireva TKh, Walker FA, Montfort WR. Heme-assisted S-nitrosation of a proximal thiolate in a nitric oxide transport protein. Proc Natl Acad Sci U S A. 2005 Jan 18;102(3):594-9. Epub 2005 Jan 6. PMID:15637157

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/1y21"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of Cimex Nitrophorin NO Complex==
-<StructureSection load='1y21' size='340' side='right' caption='[[1y21]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
+<StructureSection load='1y21' size='340' side='right'caption='[[1y21]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1y21]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Acanthia_lectularia Acanthia lectularia]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1nzh 1nzh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y21 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Y21 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1y21]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cimex_lectularius Cimex lectularius]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1nzh 1nzh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y21 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y21 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NO:NITRIC+OXIDE'>NO</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene><br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ntf|1ntf]], [[1si6|1si6]]</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>, <scene name='pdbligand=NO:NITRIC+OXIDE'>NO</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y21 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1y21 RCSB], [http://www.ebi.ac.uk/pdbsum/1y21 PDBsum]</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=1y21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y21 OCA], [https://pdbe.org/1y21 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y21 RCSB], [https://www.ebi.ac.uk/pdbsum/1y21 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y21 ProSAT]</span></td></tr>
-<table>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/NP_CIMLE NP_CIMLE] Heme-based protein that delivers nitric oxide gas (NO) to the victim while feeding, resulting in vasodilation (Probable). In place of heme, the heme-binding cysteine can also reversibly bind NO when it is present in high concentrations (PubMed:15637157).<ref>PMID:15637157</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/y2/1y21_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/y2/1y21_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</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/chain_selection.php?pdb_ID=2ata 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=1y21 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 25: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1y21" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Nitrophorin|Nitrophorin]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Acanthia lectularia]]
+[[Category: Cimex lectularius]]
-[[Category: Andersen, J F.]]
+[[Category: Large Structures]]
-[[Category: Maes, E M.]]
+[[Category: Andersen JF]]
-[[Category: Montfort, W R.]]
+[[Category: Maes EM]]
-[[Category: Shokhireva, T K.]]
+[[Category: Montfort WR]]
-[[Category: Valenzuela, J G.]]
+[[Category: Shokhireva TK]]
-[[Category: Walker, F A.]]
+[[Category: Valenzuela JG]]
-[[Category: Weichsel, A.]]
+[[Category: Walker FA]]
-[[Category: Beta-sandwich]]
+[[Category: Weichsel A]]
-[[Category: Ferrous no complex]]
-[[Category: Heme protein]]
-[[Category: Ligand binding protein]]
-[[Category: No carrier]]
-[[Category: S-nitrosocysteine]]

1y21

From Proteopedia

Current revision

Crystal Structure of Cimex Nitrophorin NO Complex

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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