人PACSIN 1蛋白的结晶及初步X射线晶体学分析
Crystallization and preliminary X-ray crystallographic analysis of human PACSIN 1 protein.
作者信息
Bai Xiaoyun, Meng Geng, Li Guoming, Luo Ming, Zheng Xiaofeng
机构信息
National Laboratory of Protein Engineering and Plant Genetic Engineering, College of Life Sciences, Peking University, Beijing 100871, People's Republic of China.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jan 1;66(Pt 1):73-5. doi: 10.1107/S1744309109049549. Epub 2009 Dec 25.
PACSIN 1, which is mainly detected in brain tissue, is one of the PACSIN-family proteins involved in endocytosis and recruitment of synaptic vesicles. It binds to dynamin, synaptojanin 1 and N-WASP, and functions in vesicle formation and transport. However, the mechanisms of action of PACSIN 1 in these processes are largely unknown. Here, full-length and five C-terminal truncation constructs of human PACSIN 1 have been successfully expressed and purified in Escherichia coli. PACSIN 1 (1-344) was crystallized and diffracted to a resolution of 3.0 A. The crystal belonged to space group C2, with unit-cell parameters a = 158.65, b = 87.38, c = 91.76 A, alpha = 90.00, beta = 113.61, gamma = 90.00 degrees . There were two molecules in the asymmetric unit and the solvent content was estimated to be about 70.47%.
PACSIN 1主要在脑组织中被检测到，是参与内吞作用和突触小泡募集的PACSIN家族蛋白之一。它与发动蛋白、突触素1和N-WASP结合，并在囊泡形成和运输中发挥作用。然而，PACSIN 1在这些过程中的作用机制在很大程度上尚不清楚。在这里，人PACSIN 1的全长和五个C末端截短构建体已在大肠杆菌中成功表达和纯化。PACSIN 1（1-344）结晶并衍射至3.0埃的分辨率。晶体属于空间群C2，晶胞参数为a = 158.65，b = 87.38，c = 91.76埃，α = 90.00，β = 113.61，γ = 90.00度。不对称单元中有两个分子，溶剂含量估计约为70.47%。
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