Three alternative conformational states of the ATP-γS-bound human 26S proteasome, visualized by cryo-electron microscopy at near-atomic resolutions. The dataset, from a study by Yanan Zhu of Peking University, captures the nucleotide-driven remodeling of the AAA-ATPase channel controlling substrate translocation gate opening.
Use Cases
- Modeling allosteric coordination within the proteasome holoenzyme based on described conformational states.
- Simulating substrate translocation mechanisms based on the described pore loop transitions between spiral staircase and saddle-shaped circle topologies.
- Analyzing nucleotide-driven gating of the core particle based on the reported asymmetric gate opening.
- Training models to predict AAA-ATPase ring conformations based on nucleotide binding states.
Strengths
- Visualized at near-atomic resolutions via cryo-EM.
- Captures three distinct alternative states of the human proteasome.
- Focuses on the nucleotide-bound (ATP-γS) condition.
Limitations
- Row count and dataset size are 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
- Peking University
- Collection Method
- Cryo-electron microscopy visualization of the human 26S proteasome.