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• W1988664574 abstract "Some viral proteins involved in interaction with the host cell surface adopt a very rigid and stable triple–β-helix fold. In order to attain this complex fold, these proteins contain an intramolecular chaperone domain that is auto-cleaved after assembly. Now structural work on two such chaperone domains indicates how they can promote correct folding of the β-helices. Protein folding is often mediated by molecular chaperones. Recently, a novel class of intramolecular chaperones has been identified in tailspike proteins of evolutionarily distant viruses, which require a C-terminal chaperone for correct folding. The highly homologous chaperone domains are interchangeable between pre-proteins and release themselves after protein folding. Here we report the crystal structures of two intramolecular chaperone domains in either the released or the pre-cleaved form, revealing the role of the chaperone domain in the formation of a triple–β-helix fold. Tentacle-like protrusions enclose the polypeptide chains of the pre-protein during the folding process. After the assembly, a sensory mechanism for correctly folded β-helices triggers a serine-lysine catalytic dyad to autoproteolytically release the mature protein. Sequence analysis shows a conservation of the intramolecular chaperones in functionally unrelated proteins sharing β-helices as a common structural motif." @default.
• W1988664574 created "2016-06-24" @default.
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• W1988664574 date "2010-01-31" @default.
• W1988664574 modified "2023-10-18" @default.
• W1988664574 title "Crystal structure of an intramolecular chaperone mediating triple–β-helix folding" @default.
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• W1988664574 doi "https://doi.org/10.1038/nsmb.1746" @default.
• W1988664574 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20118935" @default.
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