1fd9

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[[Image:1fd9.jpg|left|200px]]
 
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==CRYSTAL STRUCTURE OF THE MACROPHAGE INFECTIVITY POTENTIATOR PROTEIN (MIP) A MAJOR VIRULENCE FACTOR FROM LEGIONELLA PNEUMOPHILA==
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The line below this paragraph, containing "STRUCTURE_1fd9", creates the "Structure Box" on the page.
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<StructureSection load='1fd9' size='340' side='right'caption='[[1fd9]], [[Resolution|resolution]] 2.41&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1fd9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila Legionella pneumophila]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1FD9 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.41&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_1fd9| PDB=1fd9 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fd9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fd9 OCA], [https://pdbe.org/1fd9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fd9 RCSB], [https://www.ebi.ac.uk/pdbsum/1fd9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fd9 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MIP_LEGPH MIP_LEGPH] Essential virulence factor associated with macrophage infectivity. Exhibits PPIase activity.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fd/1fd9_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fd9 ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF THE MACROPHAGE INFECTIVITY POTENTIATOR PROTEIN (MIP) A MAJOR VIRULENCE FACTOR FROM LEGIONELLA PNEUMOPHILA'''
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==See Also==
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*[[Peptidyl-prolyl cis-trans isomerase 3D structures|Peptidyl-prolyl cis-trans isomerase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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[[Category: Large Structures]]
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==About this Structure==
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1FD9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Legionella_pneumophila Legionella pneumophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FD9 OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11524681 11524681]
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[[Category: Legionella pneumophila]]
[[Category: Legionella pneumophila]]
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[[Category: Peptidylprolyl isomerase]]
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[[Category: Fischer G]]
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[[Category: Single protein]]
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[[Category: Hacker J]]
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[[Category: Fischer, G.]]
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[[Category: Hilgenfeld R]]
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[[Category: Hacker, J]]
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[[Category: Jessen S]]
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[[Category: Hilgenfeld, R.]]
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[[Category: Konig B]]
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[[Category: Jessen, S.]]
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[[Category: Rahfeld J]]
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[[Category: Konig, B.]]
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[[Category: Riboldi-Tunnicliffe A]]
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[[Category: Rahfeld, J.]]
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[[Category: Riboldi-Tunnicliffe, A.]]
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[[Category: Dimerisation via helical interaction]]
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[[Category: Fkbp domain]]
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[[Category: Long alpha helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:11:46 2008''
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Current revision

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

PDB ID 1fd9

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