The Cupin Protein Pac13 is Suggested by the Data to Be a Homodimer.

Angewandte Chemie
Rundong Zhang

Abstract

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.

References

Dec 31, 2003·Phytochemistry·Jim M DunwellSawsan Khuri
Aug 8, 2007·Journal of Molecular Biology·Evgeny Krissinel, Kim Henrick
May 18, 2016·Proceedings of the National Academy of Sciences of the United States of America·Joanne K HobbsAlisdair B Boraston
Nov 5, 2019·Organic & Biomolecular Chemistry·Bin LiuKaifeng Hu

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