Bacterioferritins and ferritins are distantly related in evolution. Conservation of ferroxidase-centre residues.
Iron-storage proteins can be divided into two classes; the bacterioferritins and ferritins. In spite of many apparent structural and functional analogies, no significant amino acid sequence similarity has been detected previously. This report now reveals a distant evolutionary relationship between bacterioferritins and ferritins derived by 'Profile Analysis'. Optimum alignment of bacterioferritin and ferritin sequences suggests that key residues of the ferroxidase centres of ferritins are conserved in bacterioferritins.
Andrews
S C
SC
Krebs Institute for Biomolecular Research, University of Sheffield, Western Bank, UK.
Smith
J M
JM
Yewdall
S J
SJ
Guest
J R
JR
Harrison
P M
PM
D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins; D001483:Base Sequence; D002570:Ceruloplasmin / Q000235:genetics*; D003573:Cytochrome b Group / Q000235:genetics*; D016208:Databases, Factual; D004926:Escherichia coli / Q000201:enzymology; D005293:Ferritins / Q000235:genetics*; D006418:Heme / Q000737:chemistry / Q000235:genetics; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D011487:Protein Conformation; D051381:Rats; D016415:Sequence Alignment; D012689:Sequence Homology, Nucleic Acid; D014982:Xenopus laevis
D001426:Bacterial Proteins; D003573:Cytochrome b Group; D006418:Heme; D005293:Ferritins; C018032:bacterioferritin; D002570:Ceruloplasmin