title: Bacterial adhesins: structural studies reveal chaperone function and pilus biogenesis.
abstract: During the past year, remarkable progress has been made in understanding how periplasmic chaperones fold and protect protein modules that are destined for assembly into adhesive pili in Gram-negative bacteria. The first two three-dimensional structures of complexes of periplasmic chaperones with substrate pilus subunits have revealed much about the structural basis for chaperone-mediated folding and aggregation prevention, and have provided insight into the structure of adhesive pili.
authors: Swedish University of Agricultural Sciences, Uppsala Biomedical Center, Department of Molecular Biology, PO Box 590, SE 751 24, Uppsala, Sweden. stefan@xray.bmc.uu.se
authors: S D
authors: SD
authors: Knight
authors: J
authors: J
authors: Berglund
authors: D
authors: D
authors: Choudhury
mesh_terms: D018829:Adhesins, Bacterial / Q000737:chemistry*; D002241:Carbohydrates / Q000737:chemistry; D018832:Molecular Chaperones / Q000737:chemistry*; D015388:Organelles / Q000737:chemistry; D017510:Protein Folding
chemical_list: D018829:Adhesins, Bacterial; D002241:Carbohydrates; D018832:Molecular Chaperones