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'''Dlp-2 from Bacillus anthracis''' | '''Dlp-2 from Bacillus anthracis''' | ||
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[[Category: Pitulis, N.]] | [[Category: Pitulis, N.]] | ||
[[Category: Zanotti, G.]] | [[Category: Zanotti, G.]] | ||
[[Category: | [[Category: Dodecamer]] | ||
[[Category: | [[Category: Four-helix bundle]] | ||
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Revision as of 18:15, 2 May 2008
Dlp-2 from Bacillus anthracis
Overview
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.
About this Structure
1JIG is a Single protein structure of sequence from Bacillus anthracis. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 21:15:48 2008
