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2ipy

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(New page: 200px<br /> <applet load="2ipy" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ipy, resolution 2.80&Aring;" /> '''crystal structure o...)
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Revision as of 07:01, 18 November 2007

Image:2ipy.gif

2ipy, resolution 2.80Å

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crystal structure of iron regulatory protein 1 in complex with ferritin H IRE-RNA

Overview

Iron regulatory protein 1 (IRP1) binds iron-responsive elements (IREs) in, messenger RNAs (mRNAs), to repress translation or degradation, or binds an, iron-sulfur cluster, to become a cytosolic aconitase enzyme. The 2.8, angstrom resolution crystal structure of the IRP1:ferritin H IRE complex, shows an open protein conformation compared with that of cytosolic, aconitase. The extended, L-shaped IRP1 molecule embraces the IRE stem-loop, through interactions at two sites separated by approximately 30 angstroms, each involving about a dozen protein:RNA bonds. Extensive conformational, changes related to binding the IRE or an iron-sulfur cluster explain the, alternate functions of IRP1 as an mRNA regulator or enzyme.

About this Structure

2IPY is a Single protein structure of sequence from Oryctolagus cuniculus. The following page contains interesting information on the relation of 2IPY with [Aconitase and Iron Regulatory Protein 1]. Active as Aconitate hydratase, with EC number 4.2.1.3 Full crystallographic information is available from OCA.

Reference

Structure of dual function iron regulatory protein 1 complexed with ferritin IRE-RNA., Walden WE, Selezneva AI, Dupuy J, Volbeda A, Fontecilla-Camps JC, Theil EC, Volz K, Science. 2006 Dec 22;314(5807):1903-8. PMID:17185597

Page seeded by OCA on Sun Nov 18 09:08:55 2007

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