4REU
Revelation of Endogenously bound Fe2+ ions in the Crystal Structure of Ferritin from Escherichia coli
Summary for 4REU
| Entry DOI | 10.2210/pdb4reu/pdb |
| Descriptor | Ferritin, FE (III) ION, SULFATE ION, ... (8 entities in total) |
| Functional Keywords | ferritin, iron-binding, binuclear metal binding, oxidoreductase |
| Biological source | Escherichia coli str. K-12 substr. MDS42 |
| Total number of polymer chains | 6 |
| Total formula weight | 119942.67 |
| Authors | Thiruselvam, V.,Ponnuswamy, M.N.,Kumarevel, T.S. (deposition date: 2014-09-24, release date: 2014-10-22, Last modification date: 2023-11-08) |
| Primary citation | Thiruselvam, V.,Sivaraman, P.,Kumarevel, T.,Ponnuswamy, M.N. Revelation of endogenously bound Fe(2+) ions in the crystal structure of ferritin from Escherichia coli. Biochem.Biophys.Res.Commun., 453:636-641, 2014 Cited by PubMed Abstract: Ferritin is an iron regulatory protein. It is responsible for storage and detoxification of excess iron thereby it regulates iron level in the body. Here we report the crystal structure of ferritin with two endogenously expressed Fe atoms binding in both the sites. The protein was purified and characterized by MALDI-TOF and N-terminal amino acid sequencing. The crystal belongs to I4 space group and it diffracted up to 2.5Å. The structural analysis suggested that it crystallizes as hexamer and confirmed that it happened to be the first report of endogenously expressed Fe ions incorporated in both the A and B sites, situated in between the helices. PubMed: 25305494DOI: 10.1016/j.bbrc.2014.10.007 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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