3sn2
Crystal structure analysis of iron regulatory protein 1 in complex with transferrin receptor IRE B RNACrystal structure analysis of iron regulatory protein 1 in complex with transferrin receptor IRE B RNA
Structural highlights
Function[ACOC_RABIT] Iron sensor. Binds a 4Fe-4S cluster and functions as aconitase when cellular iron levels are high. Functions as mRNA binding protein that regulates uptake, sequestration and utilization of iron when cellular iron levels are low. Binds to iron-responsive elements (IRES) in target mRNA species when iron levels are low. Binding of a 4Fe-4S cluster precludes RNA binding (By similarity). Catalyzes the isomerization of citrate to isocitrate via cis-aconitate (By similarity). Publication Abstract from PubMedIron responsive elements (IREs) are short stem-loop structures found in several mRNAs encoding proteins involved in cellular iron metabolism. Iron regulatory proteins (IRPs) control iron homeostasis through differential binding to the IREs, accommodating any sequence or structural variations that the IREs may present. Here we report the structure of IRP1 in complex with transferrin receptor 1 B (TfR B) IRE, and compare it to the complex with ferritin H (Ftn H) IRE. The two IREs are bound to IRP1 through nearly identical protein-RNA contacts, although their stem conformations are significantly different. These results support the view that binding of different IREs with IRP1 depends both on protein and RNA conformational plasticity, adapting to RNA variation while retaining conserved protein-RNA contacts. Accommodating variety in iron-responsive elements: Crystal structure of transferrin receptor 1 B IRE bound to iron regulatory protein 1.,Walden WE, Selezneva A, Volz K FEBS Lett. 2012 Jan 2;586(1):32-5. Epub 2011 Nov 24. PMID:22119729[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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