Structural basis for a natural circular permutation in proteins
S. G. Nonis, J. Haywood, J. W. Schmidberger, C. S. Bond, J. S. Mylne
This study elucidates the structural basis of a natural circular permutation in conA, showing how CeAEP1 catalyzes cleavage and transpeptidation to form the stable conA protein.
bioRxiv · Oct 28, 2020 · PreprintBiochemistry