1JIG
Dlp-2 from Bacillus anthracis
Summary for 1JIG
| Entry DOI | 10.2210/pdb1jig/pdb |
| Descriptor | Dlp-2, FE (III) ION (3 entities in total) |
| Functional Keywords | dodecamer, four-helix bundle, metal transport |
| Biological source | Bacillus anthracis |
| Cellular location | Cytoplasm (By similarity): Q8RPQ1 |
| Total number of polymer chains | 4 |
| Total formula weight | 66357.70 |
| Authors | Papinutto, E.,Dundon, W.G.,Pitulis, N.,Battistutta, R.,Montecucco, C.,Zanotti, G. (deposition date: 2001-07-02, release date: 2002-06-19, Last modification date: 2024-04-03) |
| Primary citation | Papinutto, E.,Dundon, W.G.,Pitulis, N.,Battistutta, R.,Montecucco, C.,Zanotti, G. Structure of two iron-binding proteins from Bacillus anthracis. J.Biol.Chem., 277:15093-15098, 2002 Cited by PubMed Abstract: Bacillus anthracis is currently under intense investigation due to its primary importance as a human pathogen. Particularly important is the development of novel anti-anthrax vaccines, devoid of the current side effects. A novel class of immunogenic bacterial proteins consists of dodecamers homologous to the DNA-binding protein of Escherichia coli (Dps). Two Dps homologous genes are present in the B. anthracis genome. The crystal structures of these two proteins (Dlp-1 and Dlp-2) have been determined and are presented here. They are sphere-like proteins with an internal cavity. We also show that they act as ferritins and are thus involved in iron uptake and regulation, a fundamental function during bacterial growth. PubMed: 11836250DOI: 10.1074/jbc.M112378200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.46 Å) |
Structure validation
Download full validation report
