2auc

Structure of the Plasmodium MTIP-MyoA complex, a key component of the parasite invasion motor

spinqualitylabelsall models 2auc, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2auc is a 4 chain structure with sequence from Plasmodium knowlesi and Plasmodium yoelii yoelii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.6Å Ligands: MSE, SAC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D0VWV5_PLAKN 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 causative agents of malaria have developed a sophisticated machinery for entering multiple cell types in the human and insect hosts. In this machinery, a critical interaction occurs between the unusual myosin motor MyoA and the MyoA-tail Interacting Protein (MTIP). Here we present one crystal structure that shows three different conformations of Plasmodium MTIP, one of these in complex with the MyoA-tail, which reveal major conformational changes in the C-terminal domain of MTIP upon binding the MyoA-tail helix, thereby creating several hydrophobic pockets in MTIP that are the recipients of key hydrophobic side chains of MyoA. Because we also show that the MyoA helix is able to block parasite growth, this provides avenues for designing antimalarials. Structure of the MTIP-MyoA complex, a key component of the malaria parasite invasion motor.,Bosch J, Turley S, Daly TM, Bogh SM, Villasmil ML, Roach C, Zhou N, Morrisey JM, Vaidya AB, Bergman LW, Hol WG Proc Natl Acad Sci U S A. 2006 Mar 28;103(13):4852-7. Epub 2006 Mar 17. PMID:16547135 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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