Structure of dual function iron regulatory protein 1 complexed with ferritin IRE-RNA |
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Authors: | Walden William E Selezneva Anna I Dupuy Jérôme Volbeda Anne Fontecilla-Camps Juan C Theil Elizabeth C Volz Karl |
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Institution: | Department of Microbiology and Immunology, University of Illinois at Chicago, Chicago, IL 60612-7344, USA. |
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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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