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 |
Volume | 73 |
Issue | Pt 9 |
Pagination | 520-524 |
Date Published | 2017 Sep 01 |
ISSN | 2053-230X |
Keywords | Amino Acid Sequence, Bacterial Proteins, Chlorobium, Crystallization, Crystallography, X-Ray, GTP Phosphohydrolases, Models, Molecular, Protein Conformation, Protein Domains |
Abstract | 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. |
DOI | 10.1107/S2053230X17011955 |
Alternate Journal | Acta Crystallogr F Struct Biol Commun |
PubMed ID | 28876231 |
PubMed Central ID | PMC5619744 |
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