1JVW
TRYPANOSOMA CRUZI MACROPHAGE INFECTIVITY POTENTIATOR (TCMIP)
Summary for 1JVW
| Entry DOI | 10.2210/pdb1jvw/pdb |
| Descriptor | MACROPHAGE INFECTIVITY POTENTIATOR (2 entities in total) |
| Functional Keywords | macrophage infectivity potentiator, trypanosoma cruzi, chagas disease, x-ray crystal structure, rotamase, isomerase |
| Biological source | Trypanosoma cruzi |
| Cellular location | Secreted, extracellular space: Q09734 |
| Total number of polymer chains | 1 |
| Total formula weight | 18863.27 |
| Authors | Pereira, P.J.B.,Vega, M.C.,Gonzalez-Rey, E.,Fernandez-Carazo, R.,Macedo-Ribeiro, S.,Gomis-Rueth, F.X.,Gonzalez, A.,Coll, M. (deposition date: 2001-08-31, release date: 2002-06-05, Last modification date: 2024-02-07) |
| Primary citation | Pereira, P.J.,Vega, M.C.,Gonzalez-Rey, E.,Fernandez-Carazo, R.,Macedo-Ribeiro, S.,Gomis-Ruth, F.X.,Gonzalez, A.,Coll, M. Trypanosoma cruzi macrophage infectivity potentiator has a rotamase core and a highly exposed alpha-helix. EMBO Rep., 3:88-94, 2002 Cited by PubMed Abstract: The macrophage infectivity potentiator protein from Trypanosoma cruzi (TcMIP) is a major virulence factor secreted by the etiological agent of Chagas' disease. It is functionally involved in host cell invasion. We have determined the three-dimensional crystal structure of TcMIP at 1.7 A resolution. The monomeric protein displays a peptidyl-prolyl cis-trans isomerase (PPIase) core, encompassing the characteristic rotamase hydrophobic active site, thus explaining the strong inhibition of TcMIP by the immunosuppressant FK506 and related drugs. In TcMIP, the twisted beta-sheet of the core is extended by an extra beta-strand, preceded by a long, exposed N-terminal alpha-helix, which might be a target recognition element. An invasion assay shows that the MIP protein from Legionella pneumophila (LpMIP), which has an equivalent N-terminal alpha-helix, can substitute for TcMIP. An additional exposed alpha-helix, this one unique to TcMIP, is located in the C-terminus of the protein. The high-resolution structure reported here opens the possibility for the design of new inhibitory drugs that might be useful for the clinical treatment of American trypanosomiasis. PubMed: 11751578DOI: 10.1093/embo-reports/kvf009 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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