4AOM
MTIP and MyoA complex
Summary for 4AOM
| Entry DOI | 10.2210/pdb4aom/pdb |
| Descriptor | MYOSIN A TAIL DOMAIN INTERACTING PROTEIN, MYOSIN-A (3 entities in total) |
| Functional Keywords | membrane protein-motor protein complex, membrane protein/motor protein |
| Biological source | PLASMODIUM FALCIPARUM More |
| Cellular location | Cell membrane ; Peripheral membrane protein ; Cytoplasmic side : Q9UAR6 |
| Total number of polymer chains | 2 |
| Total formula weight | 18839.18 |
| Authors | Salgado, P.S.,Douse, C.H.,Simpson, P.J.,Thomas, J.C.,Holder, A.A.,Tate, E.W.,Cota, E. (deposition date: 2012-03-29, release date: 2012-09-05, Last modification date: 2023-12-20) |
| Primary citation | Douse, C.H.,Green, J.L.,Salgado, P.S.,Simpson, P.J.,Thomas, J.C.,Holder, A.A.,Tate, E.W.,Cota, E. Regulation of the Plasmodium Motor Complex: Phosphorylation of Myosin a Tail Interacting Protein (Mtip) Loosens its Grip on Myoa J.Biol.Chem., 287:36968-, 2012 Cited by PubMed Abstract: The 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. PubMed: 22932904DOI: 10.1074/JBC.M112.379842 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.939 Å) |
Structure validation
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