1jig
Dlp-2 from Bacillus anthracisDlp-2 from Bacillus anthracis
Structural highlights
Function[DPS1_BACAN] Protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton Fe(2+) ion (By similarity). It is capable of binding and sequestering Fe(2+) ion. Does not bind DNA. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBacillus 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. Structure of two iron-binding proteins from Bacillus anthracis.,Papinutto E, Dundon WG, Pitulis N, Battistutta R, Montecucco C, Zanotti G J Biol Chem. 2002 Apr 26;277(17):15093-8. Epub 2002 Feb 8. PMID:11836250[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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