3ka6

Frog M-ferritin, EED mutant, with cobaltFrog M-ferritin, EED mutant, with cobalt

Structural highlights 3ka6 is a 1 chain structure with sequence from American bullfrog. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , , Related: 3ka3, 3ka4, 3ka8, 3ka9 Activity: Ferroxidase, with EC number 1.16.3.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [FRI2_LITCT] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Ferritin nanocages synthesize ferric oxide minerals, containing hundreds to thousands of Fe(III) diferric oxo/hydroxo complexes, by reactions of Fe(II) ions with O(2) at multiple di-iron catalytic centers. Ferric-oxy multimers, tetramers, and/or larger mineral nuclei form during postcatalytic transit through the protein cage, and mineral accretion occurs in the central cavity. We determined how Fe(II) substrates can access catalytic sites using frog M ferritins, active and inactivated by ligand substitution, crystallized with 2.0 M Mg(II) +/- 0.1 M Co(II) for Co(II)-selective sites. Co(II) inhibited Fe(II) oxidation. High-resolution (<1.5 A) crystal structures show (1) a line of metal ions, 15 A long, which penetrates the cage and defines ion channels and internal pores to the nanocavity that link external pores to the cage interior, (2) metal ions near negatively charged residues at the channel exits and along the inner cavity surface that model Fe(II) transit to active sites, and (3) alternate side-chain conformations, absent in ferritins with catalysis eliminated by amino acid substitution, which support current models of protein dynamics and explain changes in Fe-Fe distances observed during catalysis. The new structural data identify a approximately 27-A path Fe(II) ions can follow through ferritin entry channels between external pores and the central cavity and along the cavity surface to the active sites where mineral synthesis begins. This "bucket brigade" for Fe(II) ion access to the ferritin catalytic sites not only increases understanding of biological nanomineral synthesis but also reveals unexpected design principles for protein cage-based catalysts and nanomaterials. Moving metal ions through ferritin-protein nanocages from three-fold pores to catalytic sites.,Tosha T, Ng HL, Bhattasali O, Alber T, Theil EC J Am Chem Soc. 2010 Oct 20;132(41):14562-9. PMID:20866049 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ferritin

spinqualitylabelsall models 3ka6, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image