Download MendeleyStructure of two iron-binding proteins from Bacillus anthracis.
Papinutto, E., Dundon, W.G., Pitulis, N., Battistutta, R., Montecucco, C., Zanotti, G.(2002) J Biological Chem 277: 15093-15098
- PubMed: 11836250
- DOI: https://doi.org/10.1074/jbc.M112378200
- Primary Citation of Related Structures:
1JI5, 1JIG - 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.
Organizational Affiliation:
Dipartimento di Chimica Organica e Centro CNR Biopolimeri, Università di Padova, Via Marzolo 1, 35131 Padova, Italy.
