1eqd

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1eqd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eqd, resolution 1.6&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
Line 1: Line 1:
-
[[Image:1eqd.gif|left|200px]]<br /><applet load="1eqd" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1eqd.gif|left|200px]]<br /><applet load="1eqd" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1eqd, resolution 1.6&Aring;" />
caption="1eqd, resolution 1.6&Aring;" />
'''CRYSTAL STRUCTURE OF NITROPHORIN 4 COMPLEXED WITH CN'''<br />
'''CRYSTAL STRUCTURE OF NITROPHORIN 4 COMPLEXED WITH CN'''<br />
==Overview==
==Overview==
-
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.
+
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==
-
1EQD 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 CYN, HEV and CIT as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EQD OCA].
+
1EQD 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=CYN:'>CYN</scene>, <scene name='pdbligand=HEV:'>HEV</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=1EQD OCA].
==Reference==
==Reference==
Line 13: Line 13:
[[Category: Rhodnius prolixus]]
[[Category: Rhodnius prolixus]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Andersen, J.F.]]
+
[[Category: Andersen, J F.]]
-
[[Category: Montfort, W.R.]]
+
[[Category: Montfort, W R.]]
-
[[Category: Roberts, S.A.]]
+
[[Category: Roberts, S A.]]
[[Category: Weichsel, A.]]
[[Category: Weichsel, A.]]
[[Category: CIT]]
[[Category: CIT]]
Line 25: Line 25:
[[Category: lipocalin fold]]
[[Category: lipocalin fold]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:13:43 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:30:28 2008''

Revision as of 10:30, 21 February 2008

Image:1eqd.gif

1eqd, resolution 1.6Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF NITROPHORIN 4 COMPLEXED WITH CN

Overview

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

1EQD is a Single protein structure of sequence from Rhodnius prolixus with , and as ligands. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Thu Feb 21 12:30:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1eqd"
Personal tools