CSFV NS5B Crystal Structures and Fidelity Assays

2.1-2.5 Å resolution crystal structures of the classical swine fever virus NS5B protein were solved to study RNA polymerase fidelity. The dataset includes structural data from wild-type and mutant proteins, along with results from multiple in vitro RdRP assays measuring fidelity and processivity. The work was authored by Weichi Liu of the Chinese Academy of Sciences and is available via paperswithcode.

Use Cases

• Analyzing intra-molecular interactions between the N-terminal and palm domains based on high-resolution crystal structures.
• Studying the impact of specific residue mutations (e.g., Y471, E472) on polymerase fidelity using in vitro RdRP assay data.
• Comparing 'open' and 'closed' conformational states of the NS5B protein based on crystallized interface mutants.
• Investigating the co-evolution of multi-domain enzymes based on the described unique mode of fidelity modulation.

Strengths

• Includes high-resolution structural data at 2.1-2.5 Å resolution.
• Contains comparative data from designed mutations at residues Y471 and E472.
• Combines structural data with functional assays measuring fidelity and processivity.

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

paperswithcode, author Weichi Liu, Chinese Academy of Sciences

Collection Method

Crystallography and in vitro biochemical assays.