3MMI

Crystal structure of the globular tail of Myo4p

3MMI の概要

• エントリーDOI: 10.2210/pdb3mmi/pdb
• 分子名称: Myosin-4 (2 entities in total)
• 機能のキーワード: globular tail, type v myosin, dilute domain, motor protein
• 由来する生物種: Saccharomyces cerevisiae (yeast)
• 細胞内の位置: Bud: P32492
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 87973.87

構造登録者

Heuck, A.,Niessing, D. (登録日: 2010-04-19, 公開日: 2010-05-12, 最終更新日: 2024-02-21)

主引用文献

Heuck, A.,Fetka, I.,Brewer, D.N.,Huls, D.,Munson, M.,Jansen, R.P.,Niessing, D.
The structure of the Myo4p globular tail and its function in ASH1 mRNA localization.
J.Cell Biol., 189:497-510, 2010

PubMed Abstract: Type V myosin (MyoV)-dependent transport of cargo is an essential process in eukaryotes. Studies on yeast and vertebrate MyoV showed that their globular tails mediate binding to the cargo complexes. In Saccharomyces cerevisiae, the MyoV motor Myo4p interacts with She3p to localize asymmetric synthesis of HO 1 (ASH1) mRNA into the bud of dividing cells. A recent study showed that localization of GFP-MS2-tethered ASH1 particles does not require the Myo4p globular tail, challenging the supposed role of this domain. We assessed ASH1 mRNA and Myo4p distribution more directly and found that their localization is impaired in cells expressing globular tail-lacking Myo4p. In vitro studies further show that the globular tail together with a more N-terminal linker region is required for efficient She3p binding. We also determined the x-ray structure of the Myo4p globular tail and identify a conserved surface patch important for She3p binding. The structure shows pronounced similarities to membrane-tethering complexes and indicates that Myo4p may not undergo auto-inhibition of its motor domain.

PubMed: 20439999
DOI: 10.1083/jcb.201002076

実験手法

X-RAY DIFFRACTION (2.3 Å)