CMB graduate student, Chloe Adams, along with Dr. Brian Eckenroth, Emily Putnam, Dr. Sylvie Doublié, and Dr. Aimee Shen, has published her article entitled “Structural and functional analysis of the CspB protease required for Clostridium spore germination,” published in PLoS Pathogens.
“We solved the 1.6 Å structure of CspB, a protease from Clostridium perfringens, a food-poisoning pathogen closely related to Clostridium difficile,” said Ms. Adams, regarding her article, “CspB is necessary for activation of SleC, a peptidoglycan hydrolase required for germination from spores. When the structure revealed three distinct domains, we explored the role of each. We determined that the prodomain is required for proper folding (as shown by others in related enzymes) but remains associated with the enzyme, which is highly unusual, and is blocking the active site. There is a 130 amino acid insertion that forms a jelly roll beta barrel domain which confers stability and rigidity to the enzyme. The central subtilase domain looks similar to many other subtilisins, especially in the region around the active site, with around .1 Ångstrom difference in positions of the catalytic residues. Our study provides the first molecular insight into CspB activity and function.”