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Viruses 2017, 9(7), 168; doi:10.3390/v9070168

Crystal Structure of the Carboxy-Terminal Region of the Bacteriophage T4 Proximal Long Tail Fiber Protein Gp34

1
Departmento de Estructura de Macromoleculas, Centro Nacional de Biotecnologia (CNB-CSIC), Calle Darwin 3, E-28049 Madrid, Spain
2
Department of Life Science and Technology, Tokyo Institute of Technology, M6-11 2-12-1 Ookayama, Meguro-ku Tokyo 152-8550, Japan
3
Departmento Bioquimica y Biologia Molecular, Facultad de Farmacia, Universidad de Santiago de Compostela, E-15782 Santiago de Compostela, Spain
Current address: Centre de Biochimie Structurale, CNRS UMR 5048-UM-INSERM U 1054, 29 rue de Navacelles, 34090 Montpellier, France
Current address: School of Biochemistry, University of Bristol, Biomedical Sciences Building, University Walk, Clifton, Bristol BS8 1TD, UK
*
Authors to whom correspondence should be addressed.
Academic Editors: Tessa E. F. Quax, Matthias G. Fischer and Laurent Debarbieux
Received: 29 May 2017 / Revised: 23 June 2017 / Accepted: 27 June 2017 / Published: 30 June 2017
(This article belongs to the Special Issue Viruses of Microbes)
View Full-Text   |   Download PDF [4836 KB, uploaded 30 June 2017]   |  

Abstract

Long tail fibers of bacteriophage T4 are formed by proteins gp34, gp35, gp36, and gp37, with gp34 located at the phage-proximal end and gp37 at the phage-distal, receptor-binding end. We have solved the structure of the carboxy-terminal region of gp34, consisting of amino acids 894–1289, by single-wavelength anomalous diffraction and extended the structure to amino acids 744–1289 using data collected from crystals containing longer gp34-fragments. The structure reveals three repeats of a mixed α-β fibrous domain in residues 744 to 877. A triple-helical neck connects to an extended triple β-helix domain (amino acids 900–1127) punctuated by two β-prism domains. Next, a β-prism domain decorated with short helices and extended β-helices is present (residues 1146–1238), while the C-terminal end is capped with another short β-helical region and three β-hairpins. The structure provides insight into the stability of the fibrous gp34 protein. View Full-Text
Keywords: bacterial viruses; Caudovirales; Myoviridae; crystallography; fibrous protein bacterial viruses; Caudovirales; Myoviridae; crystallography; fibrous protein
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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

Granell, M.; Namura, M.; Alvira, S.; Kanamaru, S.; van Raaij, M.J. Crystal Structure of the Carboxy-Terminal Region of the Bacteriophage T4 Proximal Long Tail Fiber Protein Gp34. Viruses 2017, 9, 168.

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