Structural description of the active sites of mouse L-chain ferritin at 1.2 Å resolution

  title={Structural description of the active sites of mouse L-chain ferritin at 1.2 {\AA} resolution},
  author={Thierry Granier and B{\'e}atrice Langlois d'Estaintot and Bernard M. Gallois and Jean Marc Chevalier and Gilles Pr{\'e}cigoux and Paolo Santambrogio and Paolo Arosio},
  journal={JBIC Journal of Biological Inorganic Chemistry},
Abstract. The first ferritin structure refined at the atomic level has been achieved on recombinant mouse L-chain apoferritin (rMoLF) crystals. These latter diffract to 1.2 Å resolution under cryogenic conditions. When cryo-cooling the sample, the thermal disorder usually observed at room temperature is reduced and the low-temperature structure reveals several details concerning the protein putative active sites and their properties. Within the pores built up by the molecular three-fold… 
High-resolution X-ray structures of human apoferritin H-chain mutants correlated with their activity and metal-binding sites.
Crystal derivatives using Zn(II) as redox-stable alternative for Fe(II), allows us to characterize the different metal-binding sites and to study the importance of the distance of the two metal atoms in the ferroxidase centre.
Crystal structure and biochemical properties of the human mitochondrial ferritin and its mutant Ser144Ala.
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Crystal structure of a secreted insect ferritin reveals a symmetrical arrangement of heavy and light chains.
The 1.9A structure of a secreted insect ferritin from Trichoplusia ni is reported, which reveals equal numbers of H and L chains arranged with tetrahedral symmetry.
Folding of an Intrinsically Disordered Iron-Binding Peptide in Response to Sedimentation Revealed by Cryo-EM
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X-ray structures of ferritins and related proteins.
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Crystal Structure of Plant Ferritin Reveals a Novel Metal Binding Site That Functions as a Transit Site for Metal Transfer in Ferritin*
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Insights into the Effects on Metal Binding of the Systematic Substitution of Five Key Glutamate Ligands in the Ferritin of Escherichia coli*
Five E. coli ferritin variants and their Fe3+ and Zn2+ (a redox-stable alternative for Fe2+) derivatives are reported and single carboxyl ligand replacements in sites A, B, and C gave unique effects on metal binding, which explain the observed changes in Fe2+ oxidation rates.
Chemistry at the protein–mineral interface in L-ferritin assists the assembly of a functional (μ3-oxo)Tris[(μ2-peroxo)] triiron(III) cluster
The structures suggest a mechanism for iron mineral formation at the protein interface, and the functional significance of the observed patch of carboxylate side chains and resulting metallocluster for biomineralization emerges from the lower iron oxidation rate measured in the E60AE61AE64A variant of human L-ferritin.
Crystal Structures of Ferritin Grown by the Microbatch Method in the Presence of Agarose and Electric Field Shows Enhanced Metal Binding
The crystal structures of Horse Spleen Ferritin are reported, in which the crystals were grown by employing a novel approach adopting the microbatch experiments performed in the presence and absence of electric field using a 2% agarose pellet of CdSO4.
The C-Terminal Regions Have an Important Role in the Activity of the Ferroxidase Center and the Stability of Chlorobium tepidum Ferritin
Results indicate that the C-terminal regions have an important role in the activity of the ferroxidase center and the stability of rCtFtn.


Protein Express Purif
  • 2000
SHELXL97. University of Göttingen, Germany
  • 1997