Ectothiorhodospira Halophila HiPIP: Molecular Structure at 2.5-Angstrom Resolution

The molecular structure of a high potential iron-sulfur protein (HiPIP) from the purple photosynthetic bacterium Ectothiorhodospira halophila was determined by x-ray diffraction analysis. The structure was refined to a crystallographic R value of 18.4% and includes 71 amino acid residues, with a [4Fe-4S] cluster in a cubane-like conformation. The dataset, associated with a paper by D.R. Breiter from the University of Wisconsin–Madison, was sourced from the paperswithcode platform.

Use Cases

• Analyzing the three-dimensional conformation of a [4Fe-4S] cluster based on the cubane-like structure description.
• Comparing hydrogen bonding patterns around prosthetic groups based on the description of patterns in related proteins.
• Studying the relationship between protein secondary structure and redox potential based on the described Type I and Type II turns.
• Validating protein residue counts from crystallographic data based on the correction from 70 to 71 amino acids.

Strengths

• Structure determined at a nominal resolution of 2.5 Å.
• Refined to a crystallographic R value of 18.4%.
• Contains a corrected residue count of 71 amino acids.
• Includes specific unit cell dimensions (a=60.00 Å, b=31.94 Å, c=40.27 Å, β=100.5°).

Limitations

• Row count is 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

University of Wisconsin–Madison (D.R. Breiter), via paperswithcode.

Collection Method

X-ray diffraction analysis of protein crystals.