Cryo-electron microscopy structures reveal the polymerase fold of the essential C-Pol2/Dpb2 heterodimer from S. cerevisiae. The dataset includes structures of the isolated heterodimer and the CMG helicase-polymerase complex bound to a DNA fork, showing conformational changes upon binding. This structural data was produced by Panchali Goswami of The Francis Crick Institute and is available via Open Access.
Use Cases
- Analyzing protein-protein interactions based on the described inter-subunit contacts within the helicase-polymerase complex.
- Modeling conformational changes in the CMG helicase based on its altered structure upon polymerase binding described in the summary.
- Interpreting cellular phenotypes related to DNA replication based on the structural contacts explained in the dataset description.
- Studying the architecture of non-catalytic polymerase modules based on the revealed DNA polymerase fold in C-Pol2.
Strengths
- Includes high-resolution cryo-EM structures of two distinct biological complexes: an isolated heterodimer and a larger helicase-polymerase-DNA assembly.
- Structural data explains specific cellular phenotypes through observed inter-subunit contacts.
- Data is published under an Open Access (green) license, facilitating reuse.
Limitations
- Column-level documentation is absent; field semantics must be inferred after download.
- Row count is unknown, which may limit suitability assessment for computational analysis.
- Last update date is unknown; freshness unverified.
Provenance
- Source
- The Francis Crick Institute
- Collection Method
- Cryo-electron microscopy