1qgh
From Proteopedia
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THE X-RAY STRUCTURE OF THE UNUSUAL DODECAMERIC FERRITIN FROM LISTERIA INNOCUA, REVEALS A NOVEL INTERSUBUNIT IRON BINDING SITE.
Overview
Ferritin is characterized by a highly conserved architecture that, comprises 24 subunits assembled into a spherical cage with 432 symmetry., The only known exception is the dodecameric ferritin from Listeria, innocua. The structure of Listeria ferritin has been determined to a, resolution of 2.35 A by molecular replacement, using as a search model the, structure of Dps from Escherichia coli. The Listeria 12-mer is endowed, with 23 symmetry and displays the functionally relevant structural, features of the ferritin 24-mer, namely the negatively charged channels, along the three-fold symmetry axes that serve for iron entry into the, cavity and a negatively charged internal cavity for iron deposition. The, electron density map shows 12 iron ions on the inner surface of the hollow, core, at ... [(full description)]
About this Structure
1QGH is a [Single protein] structure of sequence from [Listeria innocua] with FE as [ligand]. Structure known Active Sites: ASA, ASB, ASC, ASD, ASE, ASF, ASG, ASH, ASI, ASJ, ASK and ASL. Full crystallographic information is available from [OCA].
Reference
The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site., Ilari A, Stefanini S, Chiancone E, Tsernoglou D, Nat Struct Biol. 2000 Jan;7(1):38-43. PMID:10625425
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