1y21

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[[Image:1y21.gif|left|200px]]<br /><applet load="1y21" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1y21.gif|left|200px]]
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caption="1y21, resolution 1.75&Aring;" />
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'''Crystal Structure of Cimex Nitrophorin NO Complex'''<br />
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{{Structure
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|PDB= 1y21 |SIZE=350|CAPTION= <scene name='initialview01'>1y21</scene>, resolution 1.75&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NO:NITROGEN+OXIDE'>NO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''Crystal Structure of Cimex Nitrophorin NO Complex'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1Y21 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cimex_lectularius Cimex lectularius] with <scene name='pdbligand=NO:'>NO</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=TRS:'>TRS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1NZH. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y21 OCA].
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1Y21 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Cimex_lectularius Cimex lectularius]. This structure supersedes the now removed PDB entry 1NZH. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y21 OCA].
==Reference==
==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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15637157 15637157]
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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]
[[Category: Cimex lectularius]]
[[Category: Cimex lectularius]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: heme protein; beta-sandwich; no carrier; ferrous no complex; s-nitrosocysteine]]
[[Category: heme protein; beta-sandwich; no carrier; ferrous no complex; s-nitrosocysteine]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:01:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:17:29 2008''

Revision as of 13:17, 20 March 2008


PDB ID 1y21

Drag the structure with the mouse to rotate
, resolution 1.75Å
Ligands: , and
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of Cimex Nitrophorin NO Complex


Overview

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.

About this Structure

1Y21 is a Single protein structure of sequence from Cimex lectularius. This structure supersedes the now removed PDB entry 1NZH. Full crystallographic information is available from OCA.

Reference

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

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