2AUC: Structure Of The Plasmodium Mtip-Myoa Complex, A Key Component Of The Parasite Invasion Motor

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.
PDB ID: 2AUCDownload
MMDB ID: 37087
PDB Deposition Date: 2005/8/27
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 2.6  Å
Source Organism:
synthetic construct
Similar Structures:
Biological Unit for 2AUC: tetrameric; determined by author
Molecular Components in 2AUC
Label Count Molecule
Proteins (4 molecules)
Myosin a Tail Interacting Protein
Molecule annotation
Myosin a
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB