1fd9
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(New page: 200px<br /><applet load="1fd9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fd9, resolution 2.41Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 12:42, 20 November 2007
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CRYSTAL STRUCTURE OF THE MACROPHAGE INFECTIVITY POTENTIATOR PROTEIN (MIP) A MAJOR VIRULENCE FACTOR FROM LEGIONELLA PNEUMOPHILA
Overview
The human pathogen Legionella pneumophila, the etiological agent of the, severe and often fatal Legionnaires' disease, produces a major virulence, factor, termed 'macrophage infectivity potentiator protein' (Mip), that is, necessary for optimal multiplication of the bacteria within human alveolar, macrophages. Mip exhibits a peptidyl prolyl cis-trans isomerase (PPIase), activity, which appears to be important for infection. Here we report the, 2.4 A crystal structure of the Mip protein from L. pneumophila, Philadelphia 1 and the 3.2 A crystal structure of its complex with the, drug FK506. Each monomer of the homodimeric protein consists of an, N-terminal dimerization module, a long (65 A) connecting alpha-helix and a, C-terminal PPIase domain exhibiting similarity to human FK506-binding, protein. In view of the recent significant increase in the number of, reported cases of Legionnaires' disease and other intracellular, infections, these structural results are of prime interest for the design, of new drugs directed against Mip proteins of intracellular pathogens.
About this Structure
1FD9 is a Single protein structure of sequence from Legionella pneumophila with ZN as ligand. Active as Peptidylprolyl isomerase, with EC number 5.2.1.8 Full crystallographic information is available from OCA.
Reference
Crystal structure of Mip, a prolylisomerase from Legionella pneumophila., Riboldi-Tunnicliffe A, Konig B, Jessen S, Weiss MS, Rahfeld J, Hacker J, Fischer G, Hilgenfeld R, Nat Struct Biol. 2001 Sep;8(9):779-83. PMID:11524681
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