4AOM

MTIP and MyoA complex

4AOM の概要

• エントリーDOI: 10.2210/pdb4aom/pdb
• 分子名称: MYOSIN A TAIL DOMAIN INTERACTING PROTEIN, MYOSIN-A (3 entities in total)
• 機能のキーワード: membrane protein-motor protein complex, membrane protein/motor protein
• 由来する生物種: PLASMODIUM FALCIPARUM; 詳細
• 細胞内の位置: Cell membrane ; Peripheral membrane protein ; Cytoplasmic side : Q9UAR6
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 18839.18

構造登録者

Salgado, P.S.,Douse, C.H.,Simpson, P.J.,Thomas, J.C.,Holder, A.A.,Tate, E.W.,Cota, E. (登録日: 2012-03-29, 公開日: 2012-09-05, 最終更新日: 2023-12-20)

主引用文献

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

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: 22932904
DOI: 10.1074/JBC.M112.379842

実験手法

X-RAY DIFFRACTION (1.939 Å)