Structure of two iron-binding proteins from Bacillus anthracis.
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.
Papinutto
Elena
E
Dipartimento di Chimica Organica e Centro CNR Biopolimeri, Università di Padova, Via Marzolo 1, 35131 Padova, Italy.
Dundon
William G
WG
Pitulis
Nea
N
Battistutta
Roberto
R
Montecucco
Cesare
C
Zanotti
Giuseppe
G
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
D002352:Carrier Proteins; D008667:Metalloproteins; D005293:Ferritins