Michel Max, Schwarten Melanie, Decker Christina, Nagel-Steger Luitgard, Willbold Dieter, Weiergräber Oliver H
a Institute of Complex Systems; ICS-6: Structural Biochemistry; Forschungszentrum Jülich; Jülich , Germany.
b Institut für Physikalische Biologie und BMFZ; Heinrich-Heine-Universität Düsseldorf ; Düsseldorf , Germany.
Autophagy. 2015;11(12):2300-8. doi: 10.1080/15548627.2015.1076605.
ATG101 is an essential component of the ULK complex responsible for initiating cellular autophagy in mammalian cells; its 3-dimensional structure and molecular function, however, are currently unclear. Here we present the X-ray structure of human ATG101. The protein displays an open HORMA domain fold. Both structural properties and biophysical evidence indicate that ATG101 is locked in this conformation, in contrast to the prototypical HORMA domain protein MAD2. Moreover, we discuss a potential mode of dimerization with ATG13 as a fundamental aspect of ATG101 function.
ATG101是ULK复合物的一个重要组成部分,负责在哺乳动物细胞中启动细胞自噬;然而,其三维结构和分子功能目前尚不清楚。在此,我们展示了人源ATG101的X射线结构。该蛋白质呈现出开放的HORMA结构域折叠。结构特性和生物物理证据均表明,与典型的HORMA结构域蛋白MAD2不同,ATG101锁定在这种构象中。此外,我们讨论了与ATG13二聚化的潜在模式,这是ATG101功能的一个基本方面。