6lp5

Structure of Sinonovacula constricta ferritinStructure of Sinonovacula constricta ferritin

Structural highlights 6lp5 is a 6 chain structure with sequence from Sinonovacula constricta. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.98Å Ligands: , , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D2JIV0_SINCO 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 Ferritins are ubiquitous iron-binding proteins that are mainly related to iron storage, detoxification and innate immunity. Here, we present the crystal structure of a marine invertebrate ferritin from Sinonovacula constricta at a resolution of 1.98 A. The S. constricta ferritin (ScFer) possessed some structural similarities with vertebrate ferritins, and they shared a well-conserved architecture composed of five alpha-helical bundles that assembled into a cage-like structure with 24-subunits. The structure of ScFer also showed iron binding sites in the 3-fold channel, ferroxidase center, and putative nucleation sites. Further, electrostatic potential calculations suggested that the electrostatic gradient of the 3-fold channel could provide a guidance mechanism for iron entering the ferritin cavity. Crystallographic characterization of ferritin from Sinonovacula constricta.,Su C, Ming T, Wu Y, Jiang Q, Huan H, Lu C, Zhou J, Li Y, Song H, Su X Biochem Biophys Res Commun. 2020 Mar 26;524(1):217-223. doi:, 10.1016/j.bbrc.2020.01.069. Epub 2020 Jan 23. PMID:31983429 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ferritin 3D structures

spinqualitylabelsall models 6lp5, resolution 1.98Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image