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The LRR-Roc-COR module of the Chlorobium tepidum Roco protein

Journal Contribution - Journal Article

Subtitle:crystallization and X-ray crystallographic analysis

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 P2 12 12 1, 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.The Roco protein from the bacterium C. tepidum has been used as a model system to investigate the structure and mechanism of the Roco protein family. Here, the crystallization and crystallographic analysis of the LRR-Roc-COR construct of the C. tepidum Roco protein are reported.

Journal: Acta Crystallographica Section F
ISSN: 2053-230X
Issue: 9
Volume: 73
Pages: 520-524
Publication year:2017
Keywords:Chlorobium tepidum, LRR-Roc-COR, Roco proteins
Authors:International