1eqd

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(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 ...)
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Revision as of 12:06, 20 November 2007

Image:1eqd.gif

1eqd, resolution 1.6Å

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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 CYN, HEV and CIT 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 Tue Nov 20 14:13:43 2007

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