Cupin proteins share a double-stranded β-helix fold, form one of the largest protein superfamilies, and possess remarkable functional diversity. They usually exist in homooligomeric states. Goss and co-workers recently reported that the cupin protein Pac13, which is a dehydratase that mediates the formation of the 3'-deoxy nucleoside of pacidamycins, is an unusual small monomer. However, a careful analysis of the biophysical and structural data provided by the authors suggests that Pac13 is in fact a homodimer, similar to many other cupin proteins.
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