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. 2006 Dec 22;314(5807):1903-8.
doi: 10.1126/science.1133116.

Structure of dual function iron regulatory protein 1 complexed with ferritin IRE-RNA

William E Walden  1 , Anna I Selezneva, Jérôme Dupuy, Anne Volbeda, Juan C Fontecilla-Camps, Elizabeth C Theil, Karl Volz
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Structure of dual function iron regulatory protein 1 complexed with ferritin IRE-RNA

William E Walden et al. Science. .

Abstract

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.

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