Bacterial adhesins: structural studies reveal chaperone function and pilusbiogenesis

During the past year, remarkable progress has been made in understanding ho w periplasmic chaperones fold and protect protein modules that are destined for assembly into adhesive pill in Gram-negative bacteria. The first two t hree-dimensional structures of complexes of periplasmic chaperones with sub strate pilus subunits have revealed much about the structural basis for cha perone-mediated folding and aggregation prevention, and have provided insig ht into the structure of adhesive pill.