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

TitleThe LRR-Roc-COR module of the Chlorobium tepidum Roco protein: crystallization and X-ray crystallographic analysis.
Publication TypeJournal Article
Year of Publication2017
AuthorsDeyaert, E., A. Kortholt, and W. Versées
JournalActa Crystallogr F Struct Biol Commun
Volume73
IssuePt 9
Pagination520-524
Date Published2017 Sep 01
ISSN2053-230X
KeywordsAmino 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.

DOI10.1107/S2053230X17011955
Alternate JournalActa Crystallogr F Struct Biol Commun
PubMed ID28876231
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