Journal of Molecular Biology, volume 337, issue 4, pages 905-915

Very Fast Folding and Association of a Trimerization Domain from Bacteriophage T4 Fibritin

Sarah Güthe ¹

Larisa Kapinos ¹

Andreas Möglich ¹

Sebastian Meier

Sebastian Meier ²

Stephan Grzesiek ²

THOMAS KIEFHABER ¹

Hide authors affiliations Show authors affiliations: 2 affiliations

Division of Biophysical Chemistry, Biozentrum der Universität Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland. |

Division of Structural Biology Biozentrum der Universität Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland. |

Publication type: Journal Article

Publication date: 2004-04-01

Elsevier

Journal: Journal of Molecular Biology

Quartile SCImago

Quartile WOS

Impact factor: 5.6

ISSN: 00222836, 10898638

DOI: 10.1016/j.jmb.2004.02.020

Copy DOI

Molecular Biology

Structural Biology

Abstract

The foldon domain constitutes the C-terminal 30 amino acid residues of the trimeric protein fibritin from bacteriophage T4. Its function is to promote folding and trimerization of fibritin. We investigated structure, stability and folding mechanism of the isolated foldon domain. The domain folds into the same trimeric beta-propeller structure as in fibritin and undergoes a two-state unfolding transition from folded trimer to unfolded monomers. The folding kinetics involve several consecutive reactions. Structure formation in the region of the single beta-hairpin of each monomer occurs on the submillisecond timescale. This reaction is followed by two consecutive association steps with rate constants of 1.9(+/-0.5)x10(6)M(-1)s(-1) and 5.4(+/-0.3)x10(6)M(-1)s(-1) at 0.58 M GdmCl, respectively. This is similar to the fastest reported bimolecular association reactions for folding of dimeric proteins. At low concentrations of protein, folding shows apparent third-order kinetics. At high concentrations of protein, the reaction becomes almost independent of protein concentrations with a half-time of about 3 ms, indicating that a first-order folding step from a partially folded trimer to the native protein (k=210 +/- 20 s(-1)) becomes rate-limiting. Our results suggest that all steps on the folding/trimerization pathway of the foldon domain are evolutionarily optimized for rapid and specific initiation of trimer formation during fibritin assembly. The results further show that beta-hairpins allow efficient and rapid protein-protein interactions during folding.

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Citations by publishers

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Elsevier	Elsevier, 20, 18.87% Elsevier 20 publications, 18.87%
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Springer Nature	Springer Nature, 11, 10.38% Springer Nature 11 publications, 10.38%
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American Association for the Advancement of Science (AAAS)	American Association for the Advancement of Science (AAAS), 2, 1.89% American Association for the Advancement of Science (AAAS) 2 publications, 1.89%
Royal Society of Chemistry (RSC)	Royal Society of Chemistry (RSC), 2, 1.89% Royal Society of Chemistry (RSC) 2 publications, 1.89%
Taylor & Francis	Taylor & Francis, 2, 1.89% Taylor & Francis 2 publications, 1.89%
American Society for Microbiology	American Society for Microbiology, 2, 1.89% American Society for Microbiology 2 publications, 1.89%
American Institute of Physics (AIP)	American Institute of Physics (AIP), 1, 0.94% American Institute of Physics (AIP) 1 publication, 0.94%
NEJM Group	NEJM Group, 1, 0.94% NEJM Group 1 publication, 0.94%
Biophysical Society	Biophysical Society, 1, 0.94% Biophysical Society 1 publication, 0.94%
Federation of American Societies for Experimental Biology (FASEB)	Federation of American Societies for Experimental Biology (FASEB), 1, 0.94% Federation of American Societies for Experimental Biology (FASEB) 1 publication, 0.94%
Oxford University Press	Oxford University Press, 1, 0.94% Oxford University Press 1 publication, 0.94%
American Society for Cell Biology (ASCB)	American Society for Cell Biology (ASCB), 1, 0.94% American Society for Cell Biology (ASCB) 1 publication, 0.94%
Autonomous Non-profit Organization Editorial Board of the journal Uspekhi Khimii	Autonomous Non-profit Organization Editorial Board of the journal Uspekhi Khimii, 1, 0.94% Autonomous Non-profit Organization Editorial Board of the journal Uspekhi Khimii 1 publication, 0.94%
	5 10 15 20

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GOST |

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GOST Copy

Güthe S. et al. Very Fast Folding and Association of a Trimerization Domain from Bacteriophage T4 Fibritin // Journal of Molecular Biology. 2004. Vol. 337. No. 4. pp. 905-915.

GOST all authors (up to 50) Copy

Güthe S., Kapinos L., Möglich A., Meier S., Meier S., Grzesiek S., KIEFHABER T. Very Fast Folding and Association of a Trimerization Domain from Bacteriophage T4 Fibritin // Journal of Molecular Biology. 2004. Vol. 337. No. 4. pp. 905-915.

RIS |

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RIS Copy

TY - JOUR

DO - 10.1016/j.jmb.2004.02.020

UR - https://doi.org/10.1016/j.jmb.2004.02.020

TI - Very Fast Folding and Association of a Trimerization Domain from Bacteriophage T4 Fibritin

T2 - Journal of Molecular Biology

AU - Güthe, Sarah

AU - Meier, Sebastian

AU - KIEFHABER, THOMAS

AU - Kapinos, Larisa

AU - Möglich, Andreas

AU - Meier, Sebastian

AU - Grzesiek, Stephan

PY - 2004

DA - 2004/04/01 00:00:00

PB - Elsevier

SP - 905-915

IS - 4

VL - 337

SN - 0022-2836

SN - 1089-8638

ER -

BibTex |

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BibTex Copy

@article{2004_Güthe,

author = {Sarah Güthe and Sebastian Meier and THOMAS KIEFHABER and Larisa Kapinos and Andreas Möglich and Sebastian Meier and Stephan Grzesiek},

title = {Very Fast Folding and Association of a Trimerization Domain from Bacteriophage T4 Fibritin},

journal = {Journal of Molecular Biology},

year = {2004},

volume = {337},

publisher = {Elsevier},

month = {apr},

url = {https://doi.org/10.1016/j.jmb.2004.02.020},

number = {4},

pages = {905--915},

doi = {10.1016/j.jmb.2004.02.020}

}

MLA

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MLA Copy

Güthe, Sarah, et al. “Very Fast Folding and Association of a Trimerization Domain from Bacteriophage T4 Fibritin.” Journal of Molecular Biology, vol. 337, no. 4, Apr. 2004, pp. 905-915. https://doi.org/10.1016/j.jmb.2004.02.020.

Found error?

Publisher

Elsevier

Journal

Journal of Molecular Biology

Quartile SCImago

Quartile WOS

Impact factor

5.6

ISSN

00222836 (Print)
10898638 (Electronic)