Summary for 3BKN
| Entry DOI | 10.2210/pdb3bkn/pdb |
| Descriptor | Bacterioferritin, ZINC ION, MAGNESIUM ION, ... (6 entities in total) |
| Functional Keywords | bacterioferritin, cytochrom b1, mycobacterium smegmatis, heme, iron, iron storage, metal-binding, metal binding protein |
| Biological source | Mycobacterium smegmatis str. MC2 155 |
| Total number of polymer chains | 12 |
| Total formula weight | 228663.50 |
| Authors | Janowski, R.,Auerbach-Nevo, T.,Weiss, M.S. (deposition date: 2007-12-07, release date: 2008-01-22, Last modification date: 2023-11-01) |
| Primary citation | Janowski, R.,Auerbach-Nevo, T.,Weiss, M.S. Bacterioferritin from Mycobacterium smegmatis contains zinc in its di-nuclear site. Protein Sci., 17:1138-1150, 2008 Cited by PubMed Abstract: 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. PubMed: 18445621DOI: 10.1110/ps.034819.108 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.72 Å) |
Structure validation
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