title: Knitting and snipping: chaperones in β-helix folding.
abstract: Hallmarks of proteins containing β-helices are their increased stability and rigidity and their aggregation prone folding pathways. While parallel β-helices fold independently, the folding and assembly of many triple β-helices depends on a registration signal in order to adopt the correct three-dimensional structure. In some cases this is a mere trimerization domain, in others specialized chaperones are required. Recently, the crystal structures of two classes of intramolecular chaperones of β-helical proteins have been determined. Both mediate the assembly of large tailspike proteins and release themselves after maturation; however, they differ substantially in their structure and autoproteolytic release mechanisms.
authors.affiliation: Department of Molecular Structural Biology, Institute for Microbiology and Genetics, Georg-August-University Goettingen, Justus-von-Liebig-Weg 11, 37077 Goettingen, Germany.
authors.forename: Eike C
authors.initials: EC
authors.lastname: Schulz
authors.forename: Ralf
authors.initials: R
authors.lastname: Ficner
mesh_terms: D018832:Molecular Chaperones / Q000737:chemistry* / Q000378:metabolism*; D017510:Protein Folding; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
chemical_list: D018832:Molecular Chaperones