2b3y
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(New page: 200px<br /> <applet load="2b3y" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b3y, resolution 1.85Å" /> '''Structure of a mono...)
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Revision as of 18:51, 12 November 2007
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Structure of a monoclinic crystal form of human cytosolic aconitase (IRP1)
Overview
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.
About this Structure
2B3Y is a Single protein structure of sequence from Homo sapiens with ACT, SF4, GOL and FMT as ligands. The following page contains interesting information on the relation of 2B3Y with [Aconitase and Iron Regulatory Protein 1]. Active as Aconitate hydratase, with EC number 4.2.1.3 Full crystallographic information is available from OCA.
Reference
Crystal structure of human iron regulatory protein 1 as cytosolic aconitase., Dupuy J, Volbeda A, Carpentier P, Darnault C, Moulis JM, Fontecilla-Camps JC, Structure. 2006 Jan;14(1):129-39. PMID:16407072
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