4REU: Revelation Of Endogenously Bound Fe2+ Ions In The Crystal Structure Of Ferritin From Escherichia Coli

Citation:
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 2.5A. 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.
PDB ID: 4REUDownload
MMDB ID: 124095
PDB Deposition Date: 2014/9/24
Updated in MMDB: 2014/10
Experimental Method:
x-ray diffraction
Resolution: 2.5  Å
Source Organism:
Similar Structures:
Biological Unit for 4REU: 24-meric; determined by author and by software (PISA)
Molecular Components in 4REU
Label Count Molecule
Proteins (24 molecules)
24
Ferritin
Molecule annotation
Chemicals (213 molecules)
1
48
2
69
3
4
4
88
5
4
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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