The LRR-Roc-COR module of the Chlorobium tepidum Roco protein: crystallization and X-ray crystallographic analysisDeyaert, E., Kortholt, A. & Versées, W., 1-Sep-2017, In : Acta Crystallographica Section F: Structural Biology Communications . 73, 9, p. 520-524 5 p.
Research output: Contribution to journal › Article › Academic › peer-review
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 P212121, 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.
|Number of pages||5|
|Journal||Acta Crystallographica Section F: Structural Biology Communications|
|Publication status||Published - 1-Sep-2017|
- Journal Article, PARKINSONS-DISEASE, SOLVENT CONTENT, MUTATIONS, CRYSTALS, DOMAIN