title: The aconitase family: three structural variations on a common theme.
abstract: The aconitase family contains a diverse group of iron-sulphur (Fe-S) isomerases and two types of iron regulatory protein (IRP). Structural comparisons have revealed three architecturally distinct variants in which one of the four structural domains is covalently linked at either the amino- or carboxy-terminal end of a single polypeptide or else this domain exists as an independent subunit.
authors.affiliation: Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, University of Sheffield, UK.
authors.forename: M J
authors.initials: MJ
authors.lastname: Gruer
authors.forename: P J
authors.initials: PJ
authors.lastname: Artymiuk
authors.forename: J R
authors.initials: JR
authors.lastname: Guest
mesh_terms: D000154:Aconitate Hydratase / Q000235:genetics*; D000818:Animals; D005075:Biological Evolution; D006801:Humans; D005810:Multigene Family; D010802:Phylogeny; D017434:Protein Structure, Tertiary
chemical_list: D000154:Aconitate Hydratase