| dc.creator |
Kortholt, Arjan |
|
| dc.creator |
Deyaert, Egon |
|
| dc.creator |
Versees, Wim |
|
| dc.date |
2017-09-01T00:00:00Z |
|
| dc.date.accessioned |
2023-01-09T12:02:05Z |
|
| dc.date.available |
2023-01-09T12:02:05Z |
|
| dc.identifier |
439ff117-4f59-41ca-9a63-cf3cad663fe3 |
|
| dc.identifier |
10.1107/s2053230x17011955 |
|
| dc.identifier |
https://avesis.sdu.edu.tr/publication/details/439ff117-4f59-41ca-9a63-cf3cad663fe3/oai |
|
| dc.identifier.uri |
http://acikerisim.sdu.edu.tr/xmlui/handle/123456789/97794 |
|
| dc.description |
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(1)2(1)2(1), with unit-cell parameters a = 95.6, b = 129.8, c = 179.5 angstrom, alpha = beta = gamma = 90 degrees, and diffracted to a resolution of 3.3 angstrom. 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. |
|
| dc.language |
eng |
|
| dc.rights |
info:eu-repo/semantics/closedAccess |
|
| dc.title |
The LRR-Roc-COR module of the Chlorobium tepidum Roco protein: crystallization and X-ray crystallographic analysis |
|
| dc.type |
info:eu-repo/semantics/article |
|