1fd9

<StructureSection load='1fd9' size='340' side='right' caption='[[1fd9]], [[Resolution|resolution]] 2.41&Aring;' scene=''>

<table><tr><td colspan='2'>[[1fd9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_33152 Atcc 33152]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FD9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FD9 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fd9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fd9 OCA], [http://pdbe.org/1fd9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fd9 RCSB], [http://www.ebi.ac.uk/pdbsum/1fd9 PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/MIP_LEGPN MIP_LEGPN]] Essential virulence factor associated with macrophage infectivity. Exhibits PPIase activity.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fd/1fd9_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:11524681</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1fd9" style="background-color:#fffaf0;"></div>

*[[Peptidyl-prolyl cis-trans isomerase|Peptidyl-prolyl cis-trans isomerase]]

[[Category: Atcc 33152]]

[[Category: Peptidylprolyl isomerase]]

[[Category: Fischer, G]]

[[Category: Hacker, J]]

[[Category: Hilgenfeld, R]]

[[Category: Jessen, S]]

[[Category: Konig, B]]

[[Category: Rahfeld, J]]

[[Category: Riboldi-Tunnicliffe, A]]

[[Category: Long alpha helix]]