Crystallization and preliminary X-ray diffraction data for the aconitase form of human iron-regulatory protein 1
- Laboratoire de Cristallographie et Cristallogenèse des Protéines, Institut de Biologie Structurale Jean-Pierre Ebel, CEA/CNRS/Université Joseph Fourier, Grenoble (France)
- Laboratoire de Biophysique Moléculaire et Cellulaire, Département Réponse et Dynamique Cellulaires. CEA/CNRS/Université Joseph Fourier, Grenoble (France)
- Swiss Institute for Experimental Cancer Research (ISREC), Genetics Unit, CH-1066 Epalinges (Switzerland)
Two crystal forms of the aconitase version of recombinant human IRP1 are reported. Iron-regulatory proteins (IRPs) 1 and 2 are closely related molecules involved in animal iron metabolism. Both proteins can bind to specific mRNA regions called iron-responsive elements and thereby control the expression of proteins involved in the uptake, storage and utilization of iron. In iron-replete cells, IRP1, but not IRP2, binds a [4Fe–4S] cluster and functions as a cytoplasmic aconitase, with simultaneous loss of its RNA-binding ability. Whereas IRP2 is known to be involved in Fe homeostasis, the role of IRP1 is less clear; it may provide a link between citrate and iron metabolisms and be involved in oxidative stress response. Here, two crystal forms of the aconitase version of recombinant human IRP1 are reported. An X-ray fluorescence measurement performed on a gold-derivative crystal showed the unexpected presence of zinc, in addition to gold and iron. Both native and MAD X-ray data at the Au, Fe and Zn absorption edges have been collected from these crystals.
- OSTI ID:
- 22355999
- Journal Information:
- Acta Crystallographica. Section F, Vol. 61, Issue Pt 5; Other Information: PMCID: PMC1952303; PMID: 16511074; PUBLISHER-ID: za5097; OAI: oai:pubmedcentral.nih.gov:1952303; Copyright (c) International Union of Crystallography 2005; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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