Crystallization and preliminary X-ray diffraction data for the aconitase form of human iron-regulatory protein 1.
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.
Dupuy
J
J
Laboratoire de Cristallographie et Cristallogenèse des Protéines, Institut de Biologie Structurale Jean-Pierre Ebel, CEA/CNRS/Université Joseph Fourier, Grenoble, France.
Darnault
C
C
Brazzolotto
X
X
Kühn
L C
LC
Moulis
J M
JM
Volbeda
A
A
Fontecilla-Camps
J C
JC
D000154:Aconitate Hydratase / Q000737:chemistry* / Q000378:metabolism; D003460:Crystallization; D006801:Humans; D035941:Iron Regulatory Protein 1 / Q000737:chemistry* / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D014961:X-Ray Diffraction
D011994:Recombinant Proteins; D000154:Aconitate Hydratase; D035941:Iron Regulatory Protein 1