PDBsum entry 3gw6

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Chaperone PDB id
Protein chains
(+ 0 more) 256 a.a.
PEG ×18
TAM ×3
_CL ×6
_BR ×6
Waters ×323

References listed in PDB file
Key reference
Title Crystal structure of an intramolecular chaperone mediating triple-Beta-Helix folding.
Authors E.C.Schulz, A.Dickmanns, H.Urlaub, A.Schmitt, M.Mühlenhoff, K.Stummeyer, D.Schwarzer, R.Gerardy-Schahn, R.Ficner.
Ref. Nat Struct Mol Biol, 2010, 17, 210-215.
PubMed id 20118935
Note: In the PDB file this reference is annotated as "TO BE PUBLISHED". The citation details given above have been manually determined.
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-beta-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 beta-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 beta-helices as a common structural motif.
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