3GUD

Crystal structure of a novel intramolecular chaperon

Summary for 3GUD

• Entry DOI: 10.2210/pdb3gud/pdb
• Descriptor: Neck appendage protein, BROMIDE ION, DI(HYDROXYETHYL)ETHER, ... (6 entities in total)
• Functional Keywords: 3-helix bundle, chaperon, chaperone
• Biological source: Bacillus phage GA-1 (Bacteriophage GA-1)
• Total number of polymer chains: 2
• Total formula weight: 30734.16

Authors

Schulz, E.C.,Dickmanns, A.,Ficner, R. (deposition date: 2009-03-29, release date: 2010-02-02, Last modification date: 2024-02-21)

Primary citation

Schulz, E.C.,Dickmanns, A.,Urlaub, H.,Schmitt, A.,Muhlenhoff, M.,Stummeyer, K.,Schwarzer, D.,Gerardy-Schahn, R.,Ficner, R.
Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding.
Nat.Struct.Mol.Biol., 17:210-215, 2010

PubMed Abstract: 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.

PubMed: 20118935
DOI: 10.1038/nsmb.1746

Experimental method

X-RAY DIFFRACTION (2.2 Å)