4TR9
Ternary co-crystal structure of fructose-bisphosphate aldolase from Plasmodium falciparum in complex with TRAP and a small molecule inhibitor
Summary for 4TR9
| Entry DOI | 10.2210/pdb4tr9/pdb |
| Related | 2pc4 |
| Descriptor | Fructose-bisphosphate aldolase, ALA-ALA-SER-LEU-TYR-GLU-LYS-LYS-ALA-ALA, ALA-ALA-ALA-SER-LEU-TYR-GLU-LYS-LYS-ALA-ALA, ... (6 entities in total) |
| Functional Keywords | lyase-lyase inhibitor complex, lyase/lyase inhibitor |
| Biological source | Plasmodium falciparum More |
| Total number of polymer chains | 10 |
| Total formula weight | 165823.37 |
| Authors | Bosch, G.,Weltzer, R.,O'Malley, K.,Bosch, J. (deposition date: 2014-06-15, release date: 2015-08-26, Last modification date: 2023-09-27) |
| Primary citation | Nemetski, S.M.,Cardozo, T.J.,Bosch, G.,Weltzer, R.,O'Malley, K.,Ejigiri, I.,Kumar, K.A.,Buscaglia, C.A.,Nussenzweig, V.,Sinnis, P.,Levitskaya, J.,Bosch, J. Inhibition by stabilization: targeting the Plasmodium falciparum aldolase-TRAP complex. Malar.J., 14:324-324, 2015 Cited by PubMed Abstract: Emerging resistance of the malaria parasite Plasmodium to current therapies underscores the critical importance of exploring novel strategies for disease eradication. Plasmodium species are obligate intracellular protozoan parasites. They rely on an unusual form of substrate-dependent motility for their migration on and across host-cell membranes and for host cell invasion. This peculiar motility mechanism is driven by the 'glideosome', an actin-myosin associated, macromolecular complex anchored to the inner membrane complex of the parasite. Myosin A, actin, aldolase, and thrombospondin-related anonymous protein (TRAP) constitute the molecular core of the glideosome in the sporozoite, the mosquito stage that brings the infection into mammals. PubMed: 26289816DOI: 10.1186/s12936-015-0834-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.111 Å) |
Structure validation
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