4reu

Revelation of Endogenously bound Fe2+ ions in the Crystal Structure of Ferritin from Escherichia coli

spinqualitylabelsall models 4reu, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4reu is a 6 chain structure with sequence from Escherichia coli str. K-12 substr. MDS42. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Ligands: CL, FE, HG, MES, MG, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 2.5A. 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. Revelation of endogenously bound Fe ions in the crystal structure of ferritin from Escherichia coli.,Thiruselvam V, Sivaraman P, Kumarevel T, Ponnuswamy MN Biochem Biophys Res Commun. 2014 Oct 11. pii: S0006-291X(14)01793-8. doi:, 10.1016/j.bbrc.2014.10.007. PMID:25305494 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ferritin 3D structures

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