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IRE-BP
The iron-responsive element-binding proteins, also known as IRE-BP, IRBP, IRP and IFR , bind to iron-responsive elements (IREs) in the regulation of human iron metabolism. Function ACO1, or IRP1, is a bifunctional protein that functions as an iron-responsive element (IRE)-binding protein involved in the control of iron metabolism by binding mRNA to repress translation or degradation. It functions also as the cytoplasmic isoform of aconitase. Aconitases are iron-sulfur proteins that require a 4Fe-4S cluster for their enzymatic activity, in which they catalyze conversion of citrate to isocitrate. This structure was based on x-ray crystal diffraction. The resolution was 2.80 Å. This protein was harvested from the species ''Oryctolagus cuniculus'', more commonly known as a rabbit. This protein has a couple of conformational changes associated with it to explain the alternative functions as either mRNA regulator or as an enzyme. This information was obtained from the RCSB protein da ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Aconitase
Aconitase (aconitate hydratase; ) is an enzyme that catalyses the stereo-specific isomerization of citrate to isocitrate via ''cis''- aconitate in the tricarboxylic acid cycle, a non-redox-active process. Image:Citrate wpmp.png, Image:Cis-Aconitate wpmp.png, Image:isocitric acid.svg, Structure Aconitase, displayed in the structures in the right margin of this page, has two slightly different structures, depending on whether it is activated or inactivated. In the inactive form, its structure is divided into four domains. Counting from the N-terminus, only the first three of these domains are involved in close interactions with the Fe-4Scluster, but the active site consists of residues from all four domains, including the larger C-terminal domain. The Fe-S cluster and a anion also reside in the active site. When the enzyme is activated, it gains an additional iron atom, creating a Fe-4Scluster. However, the structure of the rest of the enzyme is nearly unchanged; the c ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
