title: Structure of two iron-binding proteins from Bacillus anthracis.
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.
authors.affiliation: Dipartimento di Chimica Organica e Centro CNR Biopolimeri, Università di Padova, Via Marzolo 1, 35131 Padova, Italy.
authors.forename: Elena
authors.initials: E
authors.lastname: Papinutto
authors.forename: William G
authors.initials: WG
authors.lastname: Dundon
authors.forename: Nea
authors.initials: N
authors.lastname: Pitulis
authors.forename: Roberto
authors.initials: R
authors.lastname: Battistutta
authors.forename: Cesare
authors.initials: C
authors.lastname: Montecucco
authors.forename: Giuseppe
authors.initials: G
authors.lastname: Zanotti
mesh_terms: D000595:Amino Acid Sequence; D001408:Bacillus anthracis / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D002352:Carrier Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D003001:Cloning, Molecular; D005293:Ferritins / Q000378:metabolism; D008667:Metalloproteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D020836:Protein Structure, Quaternary; D017386:Sequence Homology, Amino Acid
chemical_list: D002352:Carrier Proteins; D008667:Metalloproteins; D005293:Ferritins