Bacterial adhesins: structural studies reveal chaperone function and pilus biogenesis.
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.
Knight
S D
SD
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
Berglund
J
J
Choudhury
D
D
D018829:Adhesins, Bacterial / Q000737:chemistry*; D002241:Carbohydrates / Q000737:chemistry; D018832:Molecular Chaperones / Q000737:chemistry*; D015388:Organelles / Q000737:chemistry; D017510:Protein Folding
D018829:Adhesins, Bacterial; D002241:Carbohydrates; D018832:Molecular Chaperones