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Viruses 2015, 7(8), 4676-4706; doi:10.3390/v7082839

Structure and Biophysical Properties of a Triple-Stranded Beta-Helix Comprising the Central Spike of Bacteriophage T4

1
Institute of Physics of Biological Systems, École Polytechnique Fédérale de Lausanne (EPFL), BSP 415, 1015 Lausanne, Switzerland
2
Service de Spectrométrie de Masse, ISIC, EPFL, BCH 1520, 1015 Lausanne, Switzerland
3
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Laboratory of Molecular Bioengineering, 16/10 Miklukho-Maklaya St., 117997 Moscow, Russia
4
Department of Biophysical Chemistry, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland
5
Department of Biological Sciences, Purdue University, 915 W. State Street, West Lafayette, IN 47907-2054, USA
6
The Research Department, Shriner's Hospital for Children, 3101 Sam Jackson Park Road, Portland, OR 97239, USA
7
Department of Biochemistry and Molecular Biology, Oregon Health and Science University, 3181 Sam Jackson Park Road, Portland, OR 97239, USA
Current address: Department of Medicine, Division of Nephrology and Hypertension, Vanderbilt University, 1161 21st Avenue South, Nashville, TN 37232, USA.
*
Authors to whom correspondence should be addressed.
Academic Editors: Rob Lavigne and Abram Aertsen
Received: 14 July 2015 / Revised: 10 August 2015 / Accepted: 13 August 2015 / Published: 18 August 2015
View Full-Text   |   Download PDF [4281 KB, uploaded 18 August 2015]   |  

Abstract

Gene product 5 (gp5) of bacteriophage T4 is a spike-shaped protein that functions to disrupt the membrane of the target cell during phage infection. Its C-terminal domain is a long and slender β-helix that is formed by three polypeptide chains wrapped around a common symmetry axis akin to three interdigitated corkscrews. The folding and biophysical properties of such triple-stranded β-helices, which are topologically related to amyloid fibers, represent an unsolved biophysical problem. Here, we report structural and biophysical characterization of T4 gp5 β-helix and its truncated mutants of different lengths. A soluble fragment that forms a dimer of trimers and that could comprise a minimal self-folding unit has been identified. Surprisingly, the hydrophobic core of the β-helix is small. It is located near the C-terminal end of the β-helix and contains a centrally positioned and hydrated magnesium ion. A large part of the β-helix interior comprises a large elongated cavity that binds palmitic, stearic, and oleic acids in an extended conformation suggesting that these molecules might participate in the folding of the complete β-helix. View Full-Text
Keywords: β-helical proteins; fibrous proteins; protein folding; X-ray crystallography; fatty acid; mass spectrometry; intrinsic protein fluorescence; protein stability; amyloid-like structure; low complexity amino acid sequence β-helical proteins; fibrous proteins; protein folding; X-ray crystallography; fatty acid; mass spectrometry; intrinsic protein fluorescence; protein stability; amyloid-like structure; low complexity amino acid sequence
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Buth, S.A.; Menin, L.; Shneider, M.M.; Engel, J.; Boudko, S.P.; Leiman, P.G. Structure and Biophysical Properties of a Triple-Stranded Beta-Helix Comprising the Central Spike of Bacteriophage T4. Viruses 2015, 7, 4676-4706.

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