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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, Vol. 17, No. 2, 02.2010, p. 210-5.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Schulz, EC, Dickmanns, A, Urlaub, H, Schmitt, A, Mühlenhoff, M, Stummeyer, K, Schwarzer, D, Gerardy-Schahn, R & Ficner, R 2010, 'Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding', NAT STRUCT MOL BIOL, vol. 17, no. 2, pp. 210-5. https://doi.org/10.1038/nsmb.1746

APA

Schulz, E. C., Dickmanns, A., Urlaub, H., Schmitt, A., Mühlenhoff, M., Stummeyer, K., Schwarzer, D., Gerardy-Schahn, R., & Ficner, R. (2010). Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding. NAT STRUCT MOL BIOL, 17(2), 210-5. https://doi.org/10.1038/nsmb.1746

Vancouver

Schulz EC, Dickmanns A, Urlaub H, Schmitt A, Mühlenhoff M, Stummeyer K et al. Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding. NAT STRUCT MOL BIOL. 2010 Feb;17(2):210-5. https://doi.org/10.1038/nsmb.1746

Bibtex

@article{11d7decdf8964a37826f1d2ab58ea8bc,
title = "Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding",
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.",
keywords = "Bacillus Phages/chemistry, Coliphages/chemistry, Crystallography, X-Ray, Models, Molecular, Molecular Chaperones/chemistry, Protein Folding, Protein Structure, Tertiary, Viral Proteins/chemistry",
author = "Schulz, {Eike C} and Achim Dickmanns and Henning Urlaub and Andreas Schmitt and Martina M{\"u}hlenhoff and Katharina Stummeyer and David Schwarzer and Rita Gerardy-Schahn and Ralf Ficner",
year = "2010",
month = feb,
doi = "10.1038/nsmb.1746",
language = "English",
volume = "17",
pages = "210--5",
journal = "NAT STRUCT MOL BIOL",
issn = "1545-9993",
publisher = "NATURE PUBLISHING GROUP",
number = "2",

}

RIS

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 -