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

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 {approx}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.

Authors:
; ; ; ; ; ;  [1];  [2];  [2]
  1. (IBS)
  2. (
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
National Institutes of Health (NIH)
OSTI Identifier:
1020593
Resource Type:
Journal Article
Journal Name:
Science
Additional Journal Information:
Journal Volume: 314; Journal Issue: 12, 2006; Journal ID: ISSN 0193-4511
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE; CONFORMATIONAL CHANGES; CRYSTAL STRUCTURE; FERRITIN; IRON; PROTEINS; RESOLUTION

Citation Formats

Walden, William E., Selezneva, Anna I., Dupuy, Jérôme, Volbeda, Anne, Fontecilla-Camps, Juan C., Theil, Elizabeth C., Volz1, Karl, CHORI), and UIC). Structure of dual function iron regulatory protein 1 complexed with ferritin IRE-RNA. United States: N. p., 2011. Web. doi:10.1126/science.1133116.
Walden, William E., Selezneva, Anna I., Dupuy, Jérôme, Volbeda, Anne, Fontecilla-Camps, Juan C., Theil, Elizabeth C., Volz1, Karl, CHORI), & UIC). Structure of dual function iron regulatory protein 1 complexed with ferritin IRE-RNA. United States. doi:10.1126/science.1133116.
Walden, William E., Selezneva, Anna I., Dupuy, Jérôme, Volbeda, Anne, Fontecilla-Camps, Juan C., Theil, Elizabeth C., Volz1, Karl, CHORI), and UIC). Wed . "Structure of dual function iron regulatory protein 1 complexed with ferritin IRE-RNA". United States. doi:10.1126/science.1133116.
@article{osti_1020593,
title = {Structure of dual function iron regulatory protein 1 complexed with ferritin IRE-RNA},
author = {Walden, William E. and Selezneva, Anna I. and Dupuy, Jérôme and Volbeda, Anne and Fontecilla-Camps, Juan C. and Theil, Elizabeth C. and Volz1, Karl and CHORI) and UIC)},
abstractNote = {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 {approx}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.},
doi = {10.1126/science.1133116},
journal = {Science},
issn = {0193-4511},
number = 12, 2006,
volume = 314,
place = {United States},
year = {2011},
month = {7}
}