2VCD
Solution structure of the FKBP-domain of Legionella pneumophila Mip in complex with rapamycin
Summary for 2VCD
| Entry DOI | 10.2210/pdb2vcd/pdb |
| NMR Information | BMRB: 15507 |
| Descriptor | Outer membrane protein MIP, RAPAMYCIN IMMUNOSUPPRESSANT DRUG (2 entities in total) |
| Functional Keywords | mip, fkbp, ppiase, membrane, rotamase, sirolimus, virulence, isomerase, rapamycin, fkbp-domain, outer membrane, legionnaires disease, macrolide antibiotic, legionella pneumophila |
| Biological source | Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513) |
| Cellular location | Cell outer membrane: Q5ZXE0 |
| Total number of polymer chains | 1 |
| Total formula weight | 15581.87 |
| Authors | Ceymann, A.,Horstmann, M.,Ehses, P.,Schweimer, K.,Paschke, A.-K.,Fischer, G.,Roesch, P.,Faber, C. (deposition date: 2007-09-20, release date: 2008-09-02, Last modification date: 2024-05-15) |
| Primary citation | Ceymann, A.,Horstmann, M.,Ehses, P.,Schweimer, K.,Paschke, A.K.,Steinert, M.,Faber, C. Solution structure of the Legionella pneumophila Mip-rapamycin complex. BMC Struct. Biol., 8:17-17, 2008 Cited by PubMed Abstract: 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. PubMed: 18366641DOI: 10.1186/1472-6807-8-17 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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