4aom | pdb_00004aom
MTIP and MyoA complex
Structural highlights
Function[MYOA_PLAFB] Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (By similarity). Publication Abstract from PubMedThe interaction between the C-terminal tail of myosin A (MyoA) and its light chain, myosin A tail domain interacting protein (MTIP), is an essential feature of the conserved molecular machinery required for gliding motility and cell invasion by apicomplexan parasites. Recent data indicate that MTIP Ser-107 and/or Ser-108 are targeted for intracellular phosphorylation. Using an optimized MyoA tail peptide to reconstitute the complex, we show that this region of MTIP is an interaction hotspot using x-ray crystallography and NMR, and S107E and S108E mutants were generated to mimic the effect of phosphorylation. NMR relaxation experiments and other biophysical measurements indicate that the S108E mutation serves to break the tight clamp around the MyoA tail, whereas S107E has a smaller but measurable impact. These data are consistent with physical interactions observed between recombinant MTIP and native MyoA from Plasmodium falciparum lysates. Taken together these data support the notion that the conserved interactions between MTIP and MyoA may be specifically modulated by this post-translational modification. Regulation of the Plasmodium Motor Complex: PHOSPHORYLATION OF MYOSIN A TAIL-INTERACTING PROTEIN (MTIP) LOOSENS ITS GRIP ON MyoA.,Douse CH, Green JL, Salgado PS, Simpson PJ, Thomas JC, Langsley G, Holder AA, Tate EW, Cota E J Biol Chem. 2012 Oct 26;287(44):36968-77. doi: 10.1074/jbc.M112.379842. Epub, 2012 Aug 29. PMID:22932904[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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