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1fd9

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Revision as of 10:46, 4 August 2021

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

Structural highlights

1fd9 is a 1 chain structure with sequence from Atcc 33152. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:	Peptidylprolyl isomerase, with EC number 5.2.1.8
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MIP_LEGPN] Essential virulence factor associated with macrophage infectivity. Exhibits PPIase activity.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Riboldi-Tunnicliffe A, Konig B, Jessen S, Weiss MS, Rahfeld J, Hacker J, Fischer G, Hilgenfeld R. Crystal structure of Mip, a prolylisomerase from Legionella pneumophila. Nat Struct Biol. 2001 Sep;8(9):779-83. PMID:11524681 doi:10.1038/nsb0901-779

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1fd9"

@@ Line 3: / Line 3: @@
 <StructureSection load='1fd9' size='340' side='right'caption='[[1fd9]], [[Resolution|resolution]] 2.41&Aring;' scene=''>
 == Structural highlights ==
-<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>
+<table><tr><td colspan='2'>[[1fd9]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/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>
+</td></tr><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>
-<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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [https://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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fd9 ProSAT]</span></td></tr>
+<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>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MIP_LEGPN MIP_LEGPN]] Essential virulence factor associated with macrophage infectivity. Exhibits PPIase activity.
+[[https://www.uniprot.org/uniprot/MIP_LEGPN MIP_LEGPN]] Essential virulence factor associated with macrophage infectivity. Exhibits PPIase activity.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 31: @@
 ==See Also==
-*[[Peptidyl-prolyl cis-trans isomerase|Peptidyl-prolyl cis-trans isomerase]]
+*[[Peptidyl-prolyl cis-trans isomerase 3D structures|Peptidyl-prolyl cis-trans isomerase 3D structures]]
 == References ==
 <references/>

1fd9

From Proteopedia

Revision as of 10:46, 4 August 2021

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

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