Publication

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

Deyaert, 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 journalArticleAcademicpeer-review

Copy link to clipboard

Documents

  • The LRR-Roc-COR module of the Chlorobium

    Final publisher's version, 1 MB, PDF-document

    Request copy

DOI

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.

Original languageEnglish
Pages (from-to)520-524
Number of pages5
JournalActa Crystallographica Section F: Structural Biology Communications
Volume73
Issue number9
Publication statusPublished - 1-Sep-2017

    Keywords

  • Journal Article, PARKINSONS-DISEASE, SOLVENT CONTENT, MUTATIONS, CRYSTALS, DOMAIN

View graph of relations

ID: 47504426