The LRR-Roc-COR module of the Chlorobium tepidum Roco protein: crystallization and X-ray crystallographic analysis


Deyaert E., Kortholt A., Versees W.

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, vol.73, pp.520-524, 2017 (Peer-Reviewed Journal) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 73
  • Publication Date: 2017
  • Doi Number: 10.1107/s2053230x17011955
  • Journal Name: ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
  • Journal Indexes: Science Citation Index Expanded, Scopus
  • Page Numbers: pp.520-524
  • Keywords: Roco proteins, Chlorobium tepidum, LRR-Roc-COR, PARKINSONS-DISEASE, SOLVENT CONTENT, MUTATIONS, CRYSTALS, DOMAIN

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 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.