Chen Xiaoyue, Xu Xuanhao, Sun Yuna, Zhou Jingwen, Ma Yuanyuan, Yan Liming, Lou Zhiyong
Laboratory of Structural Biology and MOE Laboratory of Protein Science, School of Medicine, Tsinghua University, Beijing 100084, People's Republic of China.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jan 1;68(Pt 1):69-72. doi: 10.1107/S1744309111047634. Epub 2011 Dec 24.
Plant-specific dynamin-related proteins play crucial roles in cell-plate formation, endocytosis or exocytosis, protein sorting to the vacuole and plasma membrane and the division of mitochondria and chloroplasts. In order to determine the crystal structure and thus to obtain a better understanding of the biological functions and mechanisms of dynamin-related proteins in plant cells, the GTPase domain of Arabidopsis thaliana dynamin-related protein 1A (AtDRP1A) fused to its GTPase effector domain (GED) was crystallized in a nucleotide-associated form using polyethylene glycol 3350 as precipitant. The hexagonal crystals (space group P6(1)) had unit-cell parameters a = b = 146.2, c = 204.3 Å, and diffraction data were collected to 3.6 Å resolution using synchrotron radiation. Four molecules, comprising two functional dimers, are assumed per asymmetric unit, corresponding to a Matthews coefficient of 3.9 Å(3) Da(-1) according to the molecular weight of 39 kDa.
植物特有的发动蛋白相关蛋白在细胞板形成、胞吞作用或胞吐作用、蛋白质分选至液泡和质膜以及线粒体和叶绿体分裂中发挥关键作用。为了确定晶体结构，从而更好地理解植物细胞中发动蛋白相关蛋白的生物学功能和机制，将拟南芥发动蛋白相关蛋白1A（AtDRP1A）的GTP酶结构域与其GTP酶效应结构域（GED）融合，以核苷酸结合形式，使用聚乙二醇3350作为沉淀剂进行结晶。六方晶体（空间群P6(1)）的晶胞参数为a = b = 146.2，c = 204.3 Å，利用同步辐射收集了分辨率为3.6 Å的衍射数据。每个不对称单元假定有四个分子，由两个功能二聚体组成，根据分子量39 kDa计算，马修斯系数为3.9 Å(3) Da(-1)。
