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Deciphering a novel thioredoxin-like fold family
Lisa N Kinch1, David Baker, Nick V Grishin
1Howard Hughes Medical Institute, and Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas 75390-9050, USA.
Proteins
|July 17, 2003
Summary
Researchers predicted the structure and function of a previously uncharacterized protein cluster (COG3019) using sequence and structure analysis. Findings reveal COG3019 is structurally similar to thioltransferases, suggesting a novel metal-binding active site.
Area of Science:
- Structural bioinformatics
- Protein family classification
- Computational biology
Background:
- Sequence and structure-based searches aid in identifying remote protein homologs.
- Predicting structure and function is crucial for uncharacterized protein families.
Purpose of the Study:
- To predict the structure and classify a previously uncharacterized cluster of orthologs (COG3019) within the thioredoxin-like fold superfamily.
- To identify the closest structural relatives and potential functions of COG3019.
Main Methods:
- Utilized sequence- and structure-based searching strategies.
- Employed ab initio structure prediction using Rosetta.
- Generated a global multiple-sequence alignment.
Main Results:
- Sequence and structure searches identified thioltransferases as the closest family to COG3019.
- Rosetta predicted a thioredoxin-like fold for COG3019, similar to glutaredoxin-like thioltransferase (NrdH).
- A novel active site with a CYS-X-X-CYS motif, potentially binding metal ions, was identified.
Conclusions:
- COG3019 belongs to the thioredoxin-like fold superfamily and is structurally related to thioltransferases.
- The predicted structure and conserved residues suggest a novel active site with potential metal-binding capabilities.
- This classification aids in understanding the functional roles of COG3019 within the broader thioredoxin-like fold family.