|Title||The LRR-Roc-COR module of the Chlorobium tepidum Roco protein: crystallization and X-ray crystallographic analysis.|
|Publication Type||Journal Article|
|Year of Publication||2017|
|Authors||Deyaert, E., A. Kortholt, and W. Versées|
|Journal||Acta Crystallogr F Struct Biol Commun|
|Date Published||2017 Sep 01|
|Keywords||Amino Acid Sequence, Bacterial Proteins, Chlorobium, Crystallization, Crystallography, X-Ray, GTP Phosphohydrolases, Models, Molecular, Protein Conformation, Protein Domains|
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.
|Alternate Journal||Acta Crystallogr F Struct Biol Commun|
The LRR-Roc-COR module of the Chlorobium tepidum Roco protein: crystallization and X-ray crystallographic analysis.