Cryo-EM structure of Xanthomonos oryzae transcription elongation complex with the bacterio

Chinese Academy of Sciences researchers report cryo-electron microscopy structures of bacterial transcription elongation complexes. The dataset includes 3.4 Å and 4.0 Å resolution structures of complexes containing the bacteriophage Xp10 protein P7 from the rice pathogen Xanthomonas oryzae. The structures reveal mechanisms by which P7 modulates host bacterial RNA polymerase to prevent transcription termination and inhibit initiation.

Use Cases

• Modeling protein-RNA polymerase interactions based on the described structural mechanisms.
• Studying transcription antitermination mechanisms based on the described plugging of the RNA-exit channel.
• Analyzing bacteriophage protein-mediated host regulation based on the described restraint of RNAP-clamp motions.
• Training machine learning models for protein structure prediction using the reported cryo-EM density maps.

Strengths

• Structures resolved at 3.4 Å and 4.0 Å resolution, providing atomic-level detail.
• Includes biochemical evidence supporting the structural findings described in the paper.
• Focuses on a specific bacteriophage-host system (Xp10 and Xanthomonas oryzae) with clear biological context.

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

Linlin You, Chinese Academy of Sciences

Collection Method

Cryo-electron microscopy (cryo-EM)