1FD9

CRYSTAL STRUCTURE OF THE MACROPHAGE INFECTIVITY POTENTIATOR PROTEIN (MIP) A MAJOR VIRULENCE FACTOR FROM LEGIONELLA PNEUMOPHILA

1FD9 の概要

• エントリーDOI: 10.2210/pdb1fd9/pdb
• 分子名称: PROTEIN (MACROPHAGE INFECTIVITY POTENTIATOR PROTEIN), ZINC ION (3 entities in total)
• 機能のキーワード: fkbp domain, long alpha helix, dimerisation via helical interactions, isomerase
• 由来する生物種: Legionella pneumophila
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22999.83

構造登録者

Riboldi-Tunnicliffe, A.,Jessen, S.,Konig, B.,Rahfeld, J.,Hacker, J.,Fischer, G.,Hilgenfeld, R. (登録日: 2000-07-20, 公開日: 2001-07-25, 最終更新日: 2024-02-07)

主引用文献

Riboldi-Tunnicliffe, A.,Konig, B.,Jessen, S.,Weiss, M.S.,Rahfeld, J.,Hacker, J.,Fischer, G.,Hilgenfeld, R.
Crystal structure of Mip, a prolylisomerase from Legionella pneumophila
Nat.Struct.Biol., 8:779-783, 2001

PubMed Abstract: 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.

PubMed: 11524681
DOI: 10.1038/nsb0901-779

実験手法

X-RAY DIFFRACTION (2.41 Å)