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Viruses 2015, 7(12), 6424-6440; doi:10.3390/v7122946

Structure of the Receptor-Binding Carboxy-Terminal Domain of the Bacteriophage T5 L-Shaped Tail Fibre with and without Its Intra-Molecular Chaperone

1
Departamento de Estructura de Macromoléculas, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas (CNB-CSIC), calle Darwin 3, E-28049 Madrid, Spain
2
Centro Nacional de Microbiología, ISCIII, Majadahonda, E-28220 Madrid, Spain
3
Centro Singular de Investigación en Química Biolóxica e Materiais Moleculares, Universidade de Santiago de Compostela, E-15782 Santiago de Compostela, Spain
4
Unidade de Raios X, RIAIDT, Universidade de Santiago de Compostela, E-15782 Santiago de Compostela, Spain
5
Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Univ Paris-Sud, Université Paris-Saclay, F-91198 Gif-sur-Yvette cedex, France
Current address: Department of Biochemistry, University of Zurich, CH-8057 Zurich, Switzerland
Current address: Department of Structural Biology, Center for Structural Biochemistry, F-34090 Montpellier, France
*
Author to whom correspondence should be addressed.
Academic Editors: Abram Aertsen and Rob Lavigne
Received: 29 September 2015 / Revised: 20 November 2015 / Accepted: 27 November 2015 / Published: 8 December 2015
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Abstract

Bacteriophage T5, a Siphovirus belonging to the order Caudovirales, has a flexible, three-fold symmetric tail, to which three L-shaped fibres are attached. These fibres recognize oligo-mannose units on the bacterial cell surface prior to infection and are composed of homotrimers of the pb1 protein. Pb1 has 1396 amino acids, of which the carboxy-terminal 133 residues form a trimeric intra-molecular chaperone that is auto-proteolyzed after correct folding. The structure of a trimer of residues 970–1263 was determined by single anomalous dispersion phasing using incorporated selenomethionine residues and refined at 2.3 Å resolution using crystals grown from native, methionine-containing, protein. The protein inhibits phage infection by competition. The phage-distal receptor-binding domain resembles a bullet, with the walls formed by partially intertwined beta-sheets, conferring stability to the structure. The fold of the domain is novel and the topology unique to the pb1 structure. A site-directed mutant (Ser1264 to Ala), in which auto-proteolysis is impeded, was also produced, crystallized and its 2.5 Å structure solved by molecular replacement. The additional chaperone domain (residues 1263–1396) consists of a central trimeric alpha-helical coiled-coil flanked by a mixed alpha-beta domain. Three long beta-hairpin tentacles, one from each chaperone monomer, extend into long curved grooves of the bullet-shaped domain. The chaperone-containing mutant did not inhibit infection by competition. View Full-Text
Keywords: bacterial viruses; Caudovirales; Siphoviridae; crystallography; infection; J0101 bacterial viruses; Caudovirales; Siphoviridae; crystallography; infection; J0101
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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

Garcia-Doval, C.; Castón, J.R.; Luque, D.; Granell, M.; Otero, J.M.; Llamas-Saiz, A.L.; Renouard, M.; Boulanger, P.; van Raaij, M.J. Structure of the Receptor-Binding Carboxy-Terminal Domain of the Bacteriophage T5 L-Shaped Tail Fibre with and without Its Intra-Molecular Chaperone. Viruses 2015, 7, 6424-6440.

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