Proteolysis of the type III glutamine synthetase from Bacteroides fragilis causes expedient crystal-packing rearrangements

摘要

This work details the intentional modifications that led to the first structure of a type III glutamine synthetase enzyme (GSIII). This approach followed the serendipitous discovery of digestion caused by an extracellular protease from a contaminating bacterium, Pseudomonas fluorescens. The protease only cleaves the GSIII protein at a single site, leaving the oligomer intact but allowing the protein to crystallize in a different space group. This transition from space group P1 to space group C2221 is accompanied by improved growth characteristics, more reproducible diffraction and enhanced mechanical stability. The crystallo­graphic analyses presented here provide the structural basis of the altered molecular packing in the full-length and digested crystal forms and suggest modifications for future structural studies.