RavD is a bacterial effector deubiquitinase with exquisite specificity for linear ubiquitin chains, unlike previously identified enzymes that target isopeptide-linked chains. The dataset includes the crystal structure of RavD (residues 1-200) from Legionella pneumophila strain Corby complexed with Met-1 linked di-ubiquitin. Muyang Wan from Zhejiang University authored the study, which identified RavD's role in cleaving linear Ub chains to inhibit the host NF-κB pathway during infection.
Use Cases
- Analyzing the papain-like fold and Cys-His-Ser catalytic triad of RavD based on the crystal structure description
- Studying Ub-binding surface interactions that determine Met1 linkage specificity as described in the study
- Investigating how bacterial pathogens disrupt host immune signaling via linear ubiquitin chain hydrolysis
- Using RavD as a tool to dissect linear polyubiquitin-mediated signaling pathways in mammalian cells as suggested by the research
Strengths
- Crystal structure reveals specific interacting residues determining Met1 linkage specificity
- Study identifies a unique linear ubiquitin chain-specific effector deubiquitinase from a pathogenic bacterium
Limitations
- Row count is unknown, which may limit suitability assessment
- Column-level documentation is absent; field semantics must be inferred after download
- Last update date is unknown; freshness unverified
Provenance
- Source
- paperswithcode
- Collection Method
- Extensive screening of bacterial pathogens and crystallographic analysis as described in the study