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Title: Structural Plasticity of Helical Nanotubes Based on Coiled-Coil Assemblies

Abstract

Numerous instances can be seen in evolution in which protein quaternary structures have diverged while the sequences of the building blocks have remained fairly conserved. However, the path through which such divergence has taken place is usually not known. We have designed two synthetic 29-residue α-helical peptides, based on the coiled-coil structural motif, that spontaneously self-assemble into helical nanotubes in vitro. Using electron cryomicroscopy with a newly available direct electron detection capability, we can achieve near-atomic resolution of these thin structures. We show how conservative changes of only one or two amino acids result in dramatic changes in quaternary structure, in which the assemblies can be switched between two very different forms. This system provides a framework for understanding how small sequence changes in evolution can translate into very large changes in supramolecular structure, a phenomenon that may have significant implications for the de novo design of synthetic peptide assemblies.

Authors:
 [1];  [2];  [3];  [2];  [2];  [1];  [4];  [3];  [2]
  1. Univ. of Virginia, Charlottesville, VA (United States). Dept. of Biochemistry and Molecular Genetics
  2. Emory Univ., Atlanta, GA (United States). Dept. of Chemistry
  3. Univ. of Washington, Seattle, WA (United States). Dept. of Biochemistry
  4. Emory Univ., Atlanta, GA (United States). School of Medicine, Dept. of Pediatrics
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
OSTI Identifier:
1236717
Alternate Identifier(s):
OSTI ID: 1222008; OSTI ID: 1233883
Grant/Contract Number:
W-31-109-Eng-38; ER15377; EB001567
Resource Type:
Journal Article: Published Article
Journal Name:
Structure
Additional Journal Information:
Journal Volume: 23; Journal Issue: 2; Journal ID: ISSN 0969-2126
Publisher:
Elsevier
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; electron cryo-microscopy; coiled-coils; helical polymers

Citation Formats

Egelman, Edward H., Xu, C., DiMaio, F., Magnotti, E., Modlin, C., Yu, X., Wright, E., Baker, D., and Conticello, Vincent P.. Structural Plasticity of Helical Nanotubes Based on Coiled-Coil Assemblies. United States: N. p., 2015. Web. doi:10.1016/j.str.2014.12.008.
Egelman, Edward H., Xu, C., DiMaio, F., Magnotti, E., Modlin, C., Yu, X., Wright, E., Baker, D., & Conticello, Vincent P.. Structural Plasticity of Helical Nanotubes Based on Coiled-Coil Assemblies. United States. doi:10.1016/j.str.2014.12.008.
Egelman, Edward H., Xu, C., DiMaio, F., Magnotti, E., Modlin, C., Yu, X., Wright, E., Baker, D., and Conticello, Vincent P.. Thu . "Structural Plasticity of Helical Nanotubes Based on Coiled-Coil Assemblies". United States. doi:10.1016/j.str.2014.12.008.
@article{osti_1236717,
title = {Structural Plasticity of Helical Nanotubes Based on Coiled-Coil Assemblies},
author = {Egelman, Edward H. and Xu, C. and DiMaio, F. and Magnotti, E. and Modlin, C. and Yu, X. and Wright, E. and Baker, D. and Conticello, Vincent P.},
abstractNote = {Numerous instances can be seen in evolution in which protein quaternary structures have diverged while the sequences of the building blocks have remained fairly conserved. However, the path through which such divergence has taken place is usually not known. We have designed two synthetic 29-residue α-helical peptides, based on the coiled-coil structural motif, that spontaneously self-assemble into helical nanotubes in vitro. Using electron cryomicroscopy with a newly available direct electron detection capability, we can achieve near-atomic resolution of these thin structures. We show how conservative changes of only one or two amino acids result in dramatic changes in quaternary structure, in which the assemblies can be switched between two very different forms. This system provides a framework for understanding how small sequence changes in evolution can translate into very large changes in supramolecular structure, a phenomenon that may have significant implications for the de novo design of synthetic peptide assemblies.},
doi = {10.1016/j.str.2014.12.008},
journal = {Structure},
number = 2,
volume = 23,
place = {United States},
year = {Thu Jan 22 00:00:00 EST 2015},
month = {Thu Jan 22 00:00:00 EST 2015}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record at 10.1016/j.str.2014.12.008

Citation Metrics:
Cited by: 29 works
Citation information provided by
Web of Science

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