PDBsum entry 2vcd

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Isomerase PDB id
Protein chain
137 a.a. *
* Residue conservation analysis
PDB id:
Name: Isomerase
Title: Solution structure of the fkbp-domain of legionella pneumophila mip in complex with rapamycin
Structure: Outer membrane protein mip. Chain: a. Fragment: fragment: fkbp domain, residues 97-233. Synonym: macrophage infectivity potentiator, peptidyl-prolyl cis-trans isomerase, ppiase, rotamase. Other_details: surface protein
Source: Legionella pneumophila. Organism_taxid: 446. Organ: lung. Tissue: epithelial barrier. Cell: alveolar macrophages. Other_details: alveolar macrophages can be hosts of legionella pneumophila
NMR struc: 16 models
Authors: A.Ceymann,M.Horstmann,P.Ehses,K.Schweimer,A.-K.Paschke, G.Fischer,P.Roesch,C.Faber
Key ref: A.Ceymann et al. (2008). Solution structure of the Legionella pneumophila Mip-rapamycin complex. BMC Struct Biol, 8, 17. PubMed id: 18366641
20-Sep-07     Release date:   02-Sep-08    
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Protein chain
Pfam   ArchSchema ?
Q5ZXE0  (MIP_LEGPH) -  Outer membrane protein MIP
233 a.a.
137 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     protein folding   1 term 


BMC Struct Biol 8:17 (2008)
PubMed id: 18366641  
Solution structure of the Legionella pneumophila Mip-rapamycin complex.
A.Ceymann, M.Horstmann, P.Ehses, K.Schweimer, A.K.Paschke, M.Steinert, C.Faber.
BACKGROUND: Legionella pneumphila is the causative agent of Legionnaires' disease. A major virulence factor of the pathogen is the homodimeric surface protein Mip. It shows peptidyl-prolyl cis/trans isomerase activty and is a receptor of FK506 and rapamycin, which both inhibit its enzymatic function. Insight into the binding process may be used for the design of novel Mip inhibitors as potential drugs against Legionnaires' disease. RESULTS: We have solved the solution structure of free Mip77-213 and the Mip77-213-rapamycin complex by NMR spectroscopy. Mip77-213 showed the typical FKBP-fold and only minor rearrangements upon binding of rapamycin. Apart from the configuration of a flexible hairpin loop, which is partly stabilized upon binding, the solution structure confirms the crystal structure. Comparisons to the structures of free FKBP12 and the FKBP12-rapamycin complex suggested an identical binding mode for both proteins. CONCLUSION: The structural similarity of the Mip-rapamycin and FKBP12-rapamycin complexes suggests that FKBP12 ligands may be promising starting points for the design of novel Mip inhibitors. The search for a novel drug against Legionnaires' disease may therefore benefit from the large variety of known FKBP12 inhibitors.