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Crystal structure of human iron regulatory protein 1 as cytosolic aconitase.
Structure. 2006 Jan; 14(1):129-39.S

Abstract

Iron regulatory proteins (IRPs) control the translation of proteins involved in iron uptake, storage and utilization by binding to specific noncoding sequences of the corresponding mRNAs known as iron-responsive elements (IREs). This strong interaction assures proper iron homeostasis in animal cells under iron shortage. Conversely, under iron-replete conditions, IRP1 binds a [4Fe-4S] cluster and functions as cytosolic aconitase. Regulation of the balance between the two IRP1 activities is complex, and it does not depend only on iron availability. Here, we report the crystal structure of human IRP1 in its aconitase form. Comparison with known structures of homologous enzymes reveals well-conserved folds and active site environments with significantly different surface shapes and charge distributions. The specific features of human IRP1 allow us to propose a tentative model of an IRP1-IRE complex that agrees with a range of previously obtained data.

Authors+Show Affiliations

Laboratoire de Cristallographie et de Cristallogenèse des Protéines, Institut de Biologie Structurale JP Ebel, CEA/CNRS/Université Joseph Fourier, 38027 Grenoble Cedex 1, France.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

16407072

Citation

Dupuy, Jérôme, et al. "Crystal Structure of Human Iron Regulatory Protein 1 as Cytosolic Aconitase." Structure (London, England : 1993), vol. 14, no. 1, 2006, pp. 129-39.
Dupuy J, Volbeda A, Carpentier P, et al. Crystal structure of human iron regulatory protein 1 as cytosolic aconitase. Structure. 2006;14(1):129-39.
Dupuy, J., Volbeda, A., Carpentier, P., Darnault, C., Moulis, J. M., & Fontecilla-Camps, J. C. (2006). Crystal structure of human iron regulatory protein 1 as cytosolic aconitase. Structure (London, England : 1993), 14(1), 129-39.
Dupuy J, et al. Crystal Structure of Human Iron Regulatory Protein 1 as Cytosolic Aconitase. Structure. 2006;14(1):129-39. PubMed PMID: 16407072.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystal structure of human iron regulatory protein 1 as cytosolic aconitase. AU - Dupuy,Jérôme, AU - Volbeda,Anne, AU - Carpentier,Philippe, AU - Darnault,Claudine, AU - Moulis,Jean-Marc, AU - Fontecilla-Camps,Juan Carlos, PY - 2005/08/25/received PY - 2005/09/22/revised PY - 2005/09/23/accepted PY - 2006/1/13/pubmed PY - 2006/4/14/medline PY - 2006/1/13/entrez SP - 129 EP - 39 JF - Structure (London, England : 1993) JO - Structure VL - 14 IS - 1 N2 - Iron regulatory proteins (IRPs) control the translation of proteins involved in iron uptake, storage and utilization by binding to specific noncoding sequences of the corresponding mRNAs known as iron-responsive elements (IREs). This strong interaction assures proper iron homeostasis in animal cells under iron shortage. Conversely, under iron-replete conditions, IRP1 binds a [4Fe-4S] cluster and functions as cytosolic aconitase. Regulation of the balance between the two IRP1 activities is complex, and it does not depend only on iron availability. Here, we report the crystal structure of human IRP1 in its aconitase form. Comparison with known structures of homologous enzymes reveals well-conserved folds and active site environments with significantly different surface shapes and charge distributions. The specific features of human IRP1 allow us to propose a tentative model of an IRP1-IRE complex that agrees with a range of previously obtained data. SN - 0969-2126 UR - https://www.unboundmedicine.com/medline/citation/16407072/Crystal_structure_of_human_iron_regulatory_protein_1_as_cytosolic_aconitase_ DB - PRIME DP - Unbound Medicine ER -