Mip
(macrophage infectivity potentiator)
Related genes: mip;
Keywords: Enzyme;
Structure features:
 24-kDa surface protein forms a nonglobular, V-shaped homodimer.has recently been described. Each monomer of the homodimeric protein consists of an N-terminal dimerization module, a long connecting α-helix and a C-terminal PPIase domain
PDB code :1FD9
Functions:
Necessary for intracellular survival
Mechanism:
Belongs to the enzyme family of FK-506 binding proteins that exhibit the peptidyl-prolyl-cis/trans isomerase (PPIase) activity, catalyzes the isomerization of peptide bonds N-terminal to Pro residues
References:
 Fischer G, et al., 1992. Mip protein of Legionella pneumophila exhibits peptidyl-prolyl-cis/trans isomerase (PPlase) activity. Mol. Microbiol. 6(10):1375-1383.
Cianciotto NP, Fields BS, 1992. Legionella pneumophila mip gene potentiates intracellular infection of protozoa and human macrophages. Proc. Natl. Acad. Sci. USA. 89(11):5188-5191.
Wintermeyer E, et al., 1995. Influence of site specifically altered Mip proteins on intracellular survival of Legionella pneumophila in eukaryotic cells. Infect. Immun. 63(12):4576-4583.
Swanson MS, Hammer BK, 2000. Legionella pneumophila pathogesesis: a fateful journey from amoebae to macrophages. Annu. Rev. Microbiol. 54:567-613.
Riboldi-Tunnicliffe A, et al., 2001. Crystal structure of Mip, a prolylisomerase from Legionella pneumophila. Nat. Struct. Biol. 8(9):779-783.
Helbig JH, et al., 2003. The PPIase active site of Legionella pneumophila Mip protein is involved in the infection of eukaryotic host cells. Biol. Chem. 384(1):125-137.
Kohler R, et al., 2003. Biochemical and functional analyses of the Mip protein: influence of the N-terminal half and of peptidylprolyl isomerase activity on the virulence of Legionella pneumophila. Infect. Immun. 71(8):4389-4397.
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Bacteria
