Ontology highlight
ABSTRACT:
SUBMITTER: Saio T
PROVIDER: S-EPMC4070327 | biostudies-literature | 2014 May
REPOSITORIES: biostudies-literature
Saio Tomohide T Guan Xiao X Rossi Paolo P Economou Anastassios A Kalodimos Charalampos G CG
Science (New York, N.Y.) 20140501 6184
Molecular chaperones prevent aggregation and misfolding of proteins, but scarcity of structural data has impeded an understanding of the recognition and antiaggregation mechanisms. We report the solution structure, dynamics, and energetics of three trigger factor (TF) chaperone molecules in complex with alkaline phosphatase (PhoA) captured in the unfolded state. Our data show that TF uses multiple sites to bind to several regions of the PhoA substrate protein primarily through hydrophobic contac ...[more]