Crystal structure of bullfrog M ferritin at 2.8 angstrom resolution: analysis of subunit interactions and the binuclear metal center
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY, 4(3), 243–256.
author keywords: crystallography; iron oxidation; iron storage; multisubunit proteins
MeSH headings : Amino Acid Sequence; Animals; Aspartic Acid; Binding Sites; Conserved Sequence; Crystallography, X-Ray; Ferritins / chemistry; Ferritins / metabolism; Magnesium / metabolism; Models, Molecular; Molecular Sequence Data; Protein Conformation; Rana catesbeiana; Sequence Homology, Amino Acid; Tyrosine / analysis; Tyrosine / metabolism
TL;DR:
The crystal structure of the homopolymer of recombinant frog M ferritin is determined and it is suggested that Gln137 and Asp140 are a vestige of the second GluxxHis site, resulting from single nucleotide mutations of Glu and His codons and giving rise to Ala140 or Ser140 present in other eukaryotic H-type ferritins, by additional singleucleotide mutations.
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