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5J8S

Iron-free state of Rana Catesbeiana H' ferritin variant E57A/E136A/D140A

Summary for 5J8S
Entry DOI10.2210/pdb5j8s/pdb
DescriptorFerritin, middle subunit, MAGNESIUM ION, CHLORIDE ION, ... (4 entities in total)
Functional Keywordsrana catesbeiana, ferritin variant, ferroxidase activity, m type, h' type, oxidoreductase activity, iron, oxidoreductase
Biological sourceLithobates catesbeiana (American bullfrog)
Total number of polymer chains1
Total formula weight21153.88
Authors
Pozzi, C.,Di Pisa, F.,Mangani, S.,Bernacchioni, C.,Turano, P. (deposition date: 2016-04-08, release date: 2016-10-05, Last modification date: 2024-01-10)
Primary citationBernacchioni, C.,Pozzi, C.,Di Pisa, F.,Mangani, S.,Turano, P.
Ferroxidase Activity in Eukaryotic Ferritin is Controlled by Accessory-Iron-Binding Sites in the Catalytic Cavity.
Chemistry, 22:16213-16219, 2016
Cited by
PubMed Abstract: Ferritins are iron-storage nanocage proteins that catalyze the oxidation of Fe to Fe at ferroxidase sites. By a combination of structural and spectroscopic techniques, Asp140, together with previously identified Glu57 and Glu136, is demonstrated to be an essential residue to promote the iron oxidation at the ferroxidase site. However, the presence of these three carboxylate moieties in close proximity to the catalytic centers is not essential to achieve binding of the Fe substrate to the diferric ferroxidase sites with the same coordination geometries as in the wild-type cages.
PubMed: 27650996
DOI: 10.1002/chem.201602842
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.5 Å)
Structure validation

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数据于2025-07-16公开中

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