7xz4 | pdb_00007xz4

Crystal structure of ferritin from Setaria italica

spinqualitylabelsall models 7xz4, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7xz4 is a 1 chain structure with sequence from Setaria italica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: FE, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function K3ZJM0_SETIT 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.[ARBA:ARBA00025111] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation.[RuleBase:RU361145] Publication Abstract from PubMed The extension peptide (EP) is the most distinctive feature of mature plant ferritin. Some EPs have exhibited serine-like protease activity, which is associated with iron uptake and release. EP forms a helix and a long loop, followed by a conserved core helical bundle. However, whether the EP adopts a stable or uniform folding pattern in all plants remains unclear. To clarify this, we investigated the crystal structure of ferritin-1 from Setaria italica (SiFer1), a type of monocotyledon. In our structure of SiFer1, the EP is different from other EPs in other solved structures of plant ferritins and consisted of a pair of beta-sheets, a shorter helix, and two loops, which masks two hydrophobic pockets on the outer surface of every subunit. Furthermore, sequence analysis and structure comparison suggest that the EPs in ferritins from monocotyledons may adopt a novel fold pattern, and the conformations of EPs in ferritins are alterable among different plant species. Furthermore, additional eight iron atoms were first founded binding in the fourfold channels, demonstrating the vital function of fourfold channels in iron diffusion. In all, our structure provides new clues for understanding plant ferritins and the functions of the EP. Extension Peptide of Plant Ferritin from Setaria italica Presents a Novel Fold.,Wang W, Wang Y, Xi H, Song Z, Zhang W, Xie L, Ma D, Qin N, Wang H J Agric Food Chem. 2023 Jan 11;71(1):934-943. doi: 10.1021/acs.jafc.2c07595. Epub , 2022 Dec 28. PMID:36576327 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ferritin 3D structures

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