A near-atomic-resolution cryo-electron microscopy structure reveals the assembly of the AspS-GspD pilotin-secretin complex from enterotoxigenic Escherichia coli. The structure details a 15:15 stoichiometric ratio between AspS and GspD subunits and their specific interactions. This dataset, produced by researchers at Tsinghua University, provides the first detailed structural view of this full-length complex.
Use Cases
- Modeling protein-protein interactions based on the described stoichiometry and binding interfaces.
- Training machine learning models for protein structure prediction using the near-atomic-resolution structural data.
- Analyzing membrane protein assembly mechanisms based on the detailed interaction modes described.
- Comparative structural analysis of secretion systems across bacterial species using this specific complex as a reference.
Strengths
- Provides the first near-atomic-resolution structure of a full-length Vibrio-type pilotin-secretin complex.
- Reveals a specific 15:15 stoichiometric ratio between the AspS and GspD subunits.
- Details interactions with three secondary structural elements of the GspD S domain.
Limitations
- Description metadata is limited; actual data quality requires manual inspection after download.
- Column-level documentation is absent; field semantics must be inferred after download.
- Data may reflect bias inherent to paperswithcode as a source for specialized research outputs.
Provenance
- Source
- Tsinghua University
- Collection Method
- Cryo-electron microscopy