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2ipy
From Proteopedia
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]. 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 May 4 07:45:41 2008
