1erx: Difference between revisions
New page: left|200px<br /><applet load="1erx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1erx, resolution 1.4Å" /> '''CRYSTAL STRUCTURE OF ... |
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[[Image:1erx.gif|left|200px]]<br /><applet load="1erx" size=" | [[Image:1erx.gif|left|200px]]<br /><applet load="1erx" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1erx, resolution 1.4Å" /> | caption="1erx, resolution 1.4Å" /> | ||
'''CRYSTAL STRUCTURE OF NITROPHORIN 4 COMPLEXED WITH NO'''<br /> | '''CRYSTAL STRUCTURE OF NITROPHORIN 4 COMPLEXED WITH NO'''<br /> | ||
==Overview== | ==Overview== | ||
The nitrophorins comprise an unusual family of proteins that use ferric | 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. | ||
==About this Structure== | ==About this Structure== | ||
1ERX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodnius_prolixus Rhodnius prolixus] with HEV, NO and CIT as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1ERX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodnius_prolixus Rhodnius prolixus] with <scene name='pdbligand=HEV:'>HEV</scene>, <scene name='pdbligand=NO:'>NO</scene> and <scene name='pdbligand=CIT:'>CIT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ERX OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Rhodnius prolixus]] | [[Category: Rhodnius prolixus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Andersen, J | [[Category: Andersen, J F.]] | ||
[[Category: Montfort, W | [[Category: Montfort, W R.]] | ||
[[Category: Roberts, S | [[Category: Roberts, S A.]] | ||
[[Category: Weichsel, A.]] | [[Category: Weichsel, A.]] | ||
[[Category: CIT]] | [[Category: CIT]] | ||
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[[Category: nitric oxide complex]] | [[Category: nitric oxide complex]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:30:51 2008'' | ||
Revision as of 13:30, 21 February 2008
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CRYSTAL STRUCTURE OF NITROPHORIN 4 COMPLEXED WITH NO
OverviewOverview
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.
About this StructureAbout this Structure
1ERX is a Single protein structure of sequence from Rhodnius prolixus with , and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
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
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