Structure to function relationships in ceruloplasmin: a 'moonlighting' protein.
Specialised copper sites have been recruited during evolution to provide long-range electron transfer reactivity and oxygen binding and activation in proteins destined to cope with oxygen reactivity in different organisms. Ceruloplasmin is an ancient multicopper dase evolved to insure a safe handling of oxygen in some metabolic pathways of vertebrates. The presently available knowledge of its structure provides a glimpse of its plasticity, revealing a multitude of binding sites that point to an elaborate mechanism of multifunctional activity. Ceruloplasmin represents an example of a 'moonlighting' protein that overcomes the one gene-one structure-one function concept to follow the changes of the organism in its physiological and pathological conditions.
Bielli
P
P
Institute of Microbiology and Genetics, Vienna Biocenter, University of Vienna, Austria. pamela@gem.univie.ac.at
Calabrese
L
L
D000818:Animals; D001665:Binding Sites; D002570:Ceruloplasmin / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D003300:Copper / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D013329:Structure-Activity Relationship
D003300:Copper; D002570:Ceruloplasmin