Cryo-EM Structures of Isolated S3D-Cofilin Bound to Actin Filaments

Subnanometer resolution cryo-electron microscopy maps from Yale University reveal the structure of isolated S3D-cofilin molecules bound to actin filaments. The data, authored by Andrew Huehn, provides insights into cooperative binding and filament severing mechanisms at actin-cofilactin boundaries. The structural analysis indicates local conformational changes and disruption of filament contacts.

Use Cases

• Modeling cooperative protein binding based on the described cofilin clusters.
• Studying actin filament severing mechanisms based on structural perturbations at boundaries.
• Analyzing protein-induced conformational changes based on local subunit alterations described.
• Investigating binding cooperativity based on the suggested adjacent site occupancy.

Strengths

• Subnanometer resolution maps provide high-detail structural data.
• Direct investigation of boundaries within partially decorated filaments is described.
• Analysis includes comparison of structures with different severing activities (e.g., phosphomimetic S3D-cofilin).

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

Yale University

Collection Method

Cryo-electron microscopy (cryo-EM) data analyzed at the single subunit level.