Structural highlights
Function
[A0QY79_MYCS2] Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex (By similarity).[PIRNR:PIRNR002560]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Bacterioferritins, also known as cytochrome b (1), are oligomeric iron-storage proteins consisting of 24 identical amino acid chains, which form spherical particles consisting of 24 subunits and exhibiting 432 point-group symmetry. They contain one haem b molecule at the interface between two subunits and a di-nuclear metal binding center. The X-ray structure of bacterioferritin from Mycobacterium smegmatis (Ms-Bfr) was determined to a resolution of 2.7 A in the monoclinic space group C2. The asymmetric unit of the crystals contains 12 protein molecules: five dimers and two half-dimers located along the crystallographic twofold axis. Unexpectedly, the di-nuclear metal binding center contains zinc ions instead of the typically observed iron ions in other bacterioferritins.
Bacterioferritin from Mycobacterium smegmatis contains zinc in its di-nuclear site.,Janowski R, Auerbach-Nevo T, Weiss MS Protein Sci. 2008 Jul;17(7):1138-50. Epub 2008 Apr 29. PMID:18445621[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Janowski R, Auerbach-Nevo T, Weiss MS. Bacterioferritin from Mycobacterium smegmatis contains zinc in its di-nuclear site. Protein Sci. 2008 Jul;17(7):1138-50. Epub 2008 Apr 29. PMID:18445621 doi:10.1110/ps.034819.108
