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首页> 外文期刊>EMBO Journal >Structural basis for myosin V discrimination between distinct cargoes
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Structural basis for myosin V discrimination between distinct cargoes

机译：肌凝蛋白V歧视结构依据之间不同的货物

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Myosin V molecular motors move cargoes on actin filaments. A myosin V may move multiple cargoes to distinct places at different times. The cargoes attach to the globular tail of myosin V via cargo- specific receptors. Here we report the crystal structure at 2.2 angstrom of the myosin V globular tail. The overall tertiary structure has not been previously observed. There are several patches of highly conserved regions distributed on the surface of the tail. These are candidate attachment sites for cargo- specific receptors. Indeed, we identified a region of five conserved surface residues that are solely required for vacuole inheritance. Likewise, we identified a region of five conserved surface residues that are required for secretory vesicle movement, but not vacuole movement. These two regions are at opposite ends of the oblong- shaped cargo-binding domain, and moreover are offset by 180 degrees. The fact that the cargo- binding areas are distant from each other and simultaneously exposed on the surface of the globular tail suggests that major targets for the regulation of cargo attachment are organelle- specific myosin V receptors.
机译：在肌动蛋白肌球蛋白分子马达V移动货物细丝。在不同的时间不同的地方。货物附加的球状尾肌凝蛋白V通过货物——特定的受体。肌凝蛋白的晶体结构为2.2埃V球状的尾巴。没有被观察到。的高度保守的区域分布表面的尾巴。附件为货物网站——特定的受体。事实上,我们发现了一个地区的五个守恒的只需要表面残留液泡继承。地区的五个守恒的表面残留但是,分泌囊泡运动所需吗不泡运动。椭圆形的两端——cargo-binding塑造的域,而且是抵消了180度。货物的事实——绑定区域同时远离对方接触表面的球状的尾巴表明,监管的主要目标货物附件细胞器——特定肌凝蛋白V受体。

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