Yeast Enolase Structure at 2.25-Å Resolution with Novel Beta-Alpha Barrel Topology

Lukasz Lebioda from the University of South Carolina determined the three-dimensional structure of yeast enolase using multiple isomorphous replacement and solvent flattening. The dataset describes a dimeric enzyme with an 8-fold beta+alpha-barrel domain exhibiting a novel beta beta alpha alpha (beta alpha)6 topology, refined to an R-factor of 17.0% with solvent molecules. The active site region and specific ligand residues like Asp246, Glu295, and Asp320 are detailed.

Use Cases

• Analyzing novel protein barrel topologies based on the described beta beta alpha alpha (beta alpha)6 structure.
• Studying enzyme active site architecture based on the detailed residues like Asp246, Glu295, and Asp320.
• Comparing protein domain evolution based on the structural differences between enolase and triose phosphate isomerase barrels mentioned.

Strengths

• Crystallographic refinement achieved an R-factor of 17.0% with 182 water molecules and 1 sulfate, indicating a detailed atomic model.
• The description provides specific structural dimensions (60 X 55 X 45 Å per subunit) and a clear topological description.

Limitations

• Column-level documentation is absent; field semantics must be inferred after download.
• Row count is unknown, which may limit suitability assessment.
• Last update date is unknown; freshness unverified.

Provenance

Source

University of South Carolina

Collection Method

Multiple isomorphous replacement and solvent flattening techniques from X-ray crystallography.