Structural highlights
4reu is a 6 chain structure with sequence from Escherichia coli mds42. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , , , , |
| Gene: | ftn, ECMDS42_1565 (Escherichia coli MDS42) |
| Activity: | Ferroxidase, with EC number 1.16.3.1 |
| 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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Thiruselvam V, Sivaraman P, Kumarevel T, Ponnuswamy MN. Revelation of endogenously bound Fe ions in the crystal structure of ferritin from Escherichia coli. Biochem Biophys Res Commun. 2014 Oct 11. pii: S0006-291X(14)01793-8. doi:, 10.1016/j.bbrc.2014.10.007. PMID:25305494 doi:http://dx.doi.org/10.1016/j.bbrc.2014.10.007
