Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding
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Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding. / Schulz, Eike C; Dickmanns, Achim; Urlaub, Henning; Schmitt, Andreas; Mühlenhoff, Martina; Stummeyer, Katharina; Schwarzer, David; Gerardy-Schahn, Rita; Ficner, Ralf.
in: NAT STRUCT MOL BIOL, Jahrgang 17, Nr. 2, 02.2010, S. 210-5.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding
AU - Schulz, Eike C
AU - Dickmanns, Achim
AU - Urlaub, Henning
AU - Schmitt, Andreas
AU - Mühlenhoff, Martina
AU - Stummeyer, Katharina
AU - Schwarzer, David
AU - Gerardy-Schahn, Rita
AU - Ficner, Ralf
PY - 2010/2
Y1 - 2010/2
N2 - 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.
AB - 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.
KW - Bacillus Phages/chemistry
KW - Coliphages/chemistry
KW - Crystallography, X-Ray
KW - Models, Molecular
KW - Molecular Chaperones/chemistry
KW - Protein Folding
KW - Protein Structure, Tertiary
KW - Viral Proteins/chemistry
U2 - 10.1038/nsmb.1746
DO - 10.1038/nsmb.1746
M3 - SCORING: Journal article
C2 - 20118935
VL - 17
SP - 210
EP - 215
JO - NAT STRUCT MOL BIOL
JF - NAT STRUCT MOL BIOL
SN - 1545-9993
IS - 2
ER -