6LP5

Structure of Sinonovacula constricta ferritin

Summary for 6LP5

• Entry DOI: 10.2210/pdb6lp5/pdb
• Descriptor: Ferritin, FE (II) ION, FE (III) ION, ... (5 entities in total)
• Functional Keywords: sinonovacula constricta; marine invertebrate; ferritin; metal binding sites, structural protein, oxidoreductase
• Biological source: Sinonovacula constricta (Razor clam)
• Total number of polymer chains: 6
• Total formula weight: 120073.52

Authors

Su, X.R.,Ming, T.H.,Su, C. (deposition date: 2020-01-08, release date: 2020-04-08, Last modification date: 2023-11-29)

Primary citation

Su, C.,Ming, T.,Wu, Y.,Jiang, Q.,Huan, H.,Lu, C.,Zhou, J.,Li, Y.,Song, H.,Su, X.
Crystallographic characterization of ferritin from Sinonovacula constricta.
Biochem.Biophys.Res.Commun., 524:217-223, 2020

PubMed Abstract: 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 Å. The S. constricta ferritin (ScFer) possessed some structural similarities with vertebrate ferritins, and they shared a well-conserved architecture composed of five α-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.

PubMed: 31983429
DOI: 10.1016/j.bbrc.2020.01.069

Experimental method

X-RAY DIFFRACTION (1.98 Å)