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2imq

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[[Image:2imq.jpg|left|200px]]
 
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==Crystal structure of ferrous cimex nitrophorin==
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The line below this paragraph, containing "STRUCTURE_2imq", creates the "Structure Box" on the page.
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<StructureSection load='2imq' size='340' side='right'caption='[[2imq]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2imq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cimex_lectularius Cimex lectularius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IMQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IMQ FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</td></tr>
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<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>
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{{STRUCTURE_2imq| PDB=2imq | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2imq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2imq OCA], [https://pdbe.org/2imq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2imq RCSB], [https://www.ebi.ac.uk/pdbsum/2imq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2imq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/im/2imq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2imq ConSurf].
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<div style="clear:both"></div>
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'''Crystal structure of ferrous cimex nitrophorin'''
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==See Also==
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*[[Nitrophorin|Nitrophorin]]
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== References ==
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==Overview==
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<references/>
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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.
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__TOC__
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</StructureSection>
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==About this Structure==
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2IMQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Cimex_lectularius Cimex lectularius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IMQ OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15637157 15637157]
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[[Category: Cimex lectularius]]
[[Category: Cimex lectularius]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Montfort, W R.]]
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[[Category: Montfort WR]]
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[[Category: Weichsel, A.]]
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[[Category: Weichsel A]]
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[[Category: Beta-sandwich]]
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[[Category: Ferrous heme]]
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[[Category: Transport protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:40:01 2008''
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Current revision

Crystal structure of ferrous cimex nitrophorin

PDB ID 2imq

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