Deyaert Egon, Kortholt Arjan, Versées Wim
Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium.
Department of Cell Biochemistry, University of Groningen, 9747 AG Groningen, The Netherlands.
Acta Crystallogr F Struct Biol Commun. 2017 Sep 1;73(Pt 9):520-524. doi: 10.1107/S2053230X17011955. Epub 2017 Aug 21.
Roco proteins are characterized by the presence of a Roc-COR supradomain harbouring GTPase activity, which is often preceded by an LRR domain. The most notorious member of the Roco protein family is the Parkinson's disease-associated LRRK2. The Roco protein from the bacterium Chlorobium tepidum has been used as a model system to investigate the structure and mechanism of this class of enzymes. Here, the crystallization and crystallographic analysis of the LRR-Roc-COR construct of the C. tepidum Roco protein is reported. The LRR-Roc-COR crystals belonged to space group P222, with unit-cell parameters a = 95.6, b = 129.8, c = 179.5 Å, α = β = γ = 90°, and diffracted to a resolution of 3.3 Å. Based on the calculated Matthews coefficient, Patterson map analysis and an initial molecular-replacement analysis, one protein dimer is present in the asymmetric unit. The crystal structure of this protein will provide valuable insights into the interaction between the Roc-COR and LRR domains within Roco proteins.
Roco蛋白的特征是存在具有GTPase活性的Roc-COR超结构域，该超结构域之前通常有一个LRR结构域。Roco蛋白家族中最著名的成员是与帕金森病相关的LRRK2。来自嗜热绿菌的Roco蛋白已被用作研究这类酶的结构和机制的模型系统。本文报道了嗜热绿菌Roco蛋白的LRR-Roc-COR构建体的结晶及晶体学分析。LRR-Roc-COR晶体属于空间群P222，晶胞参数a = 95.6、b = 129.8、c = 179.5 Å，α = β = γ = 90°，衍射分辨率为3.3 Å。基于计算的马修斯系数、帕特森图分析和初步的分子置换分析，不对称单元中存在一个蛋白质二聚体。该蛋白的晶体结构将为深入了解Roco蛋白中Roc-COR和LRR结构域之间的相互作用提供有价值的见解。
