Conservation of aconitase residues revealed by multiple sequence analysis. Implications for structure/function relationships.
Aconitases have recently regained much attention, because one member of this family, iron regulatory protein-1 (IRP-1), has been found to play a dual role as a cytoplasmic aconitase and a regulatory RNA-binding protein. This finding has highlighted a novel role for Fe-S clusters as post-translational regulatory switches. We have aligned 28 members of the Fe-S isomerase family, identified highly conserved amino acid residues, and integrated this information with data on the crystallographic structure of mammalian mitochondrial aconitase. We propose structural and/or functional roles for the previously unrecognized conserved residues. Our findings illustrate the value of detailed protein sequence analysis when high-resolution crystallographic data are already available.
Frishman
D
D
European Molecular Biology Laboratory, Heidelberg, Germany.
Hentze
M W
MW
D000154:Aconitate Hydratase / Q000737:chemistry* / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D017124:Conserved Sequence; D006801:Humans; D007535:Isomerases / Q000737:chemistry / Q000378:metabolism; D013329:Structure-Activity Relationship
D000154:Aconitate Hydratase; D007535:Isomerases