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

Departamento de Estructura de Macromoléculas, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas (CNB-CSIC), calle Darwin 3, E-28049 Madrid, Spain

Centro Nacional de Microbiología, ISCIII, Majadahonda, E-28220 Madrid, Spain

Centro Singular de Investigación en Química Biolóxica e Materiais Moleculares, Universidade de Santiago de Compostela, E-15782 Santiago de Compostela, Spain

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Unidade de Raios X, RIAIDT, Universidade de Santiago de Compostela, E-15782 Santiago de Compostela, Spain

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Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Univ Paris-Sud, Université Paris-Saclay, F-91198 Gif-sur-Yvette cedex, France

Author to whom correspondence should be addressed.

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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

Academic Editors: Abram Aertsen and Rob Lavigne

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

Received: 29 September 2015 / Revised: 20 November 2015 / Accepted: 27 November 2015 / Published: 8 December 2015

(This article belongs to the Special Issue 21st Evergreen International Phage Biology Meeting - Emerging Research)

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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

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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. https://doi.org/10.3390/v7122946

AMA Style

Garcia-Doval C, Castón JR, Luque D, Granell M, Otero JM, Llamas-Saiz AL, Renouard M, Boulanger P, Van Raaij MJ. 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(12):6424-6440. https://doi.org/10.3390/v7122946

Chicago/Turabian Style

Garcia-Doval, Carmela, José R. Castón, Daniel Luque, Meritxell Granell, José M. Otero, Antonio L. Llamas-Saiz, Madalena Renouard, Pascale Boulanger, and Mark J. Van Raaij. 2015. "Structure of the Receptor-Binding Carboxy-Terminal Domain of the Bacteriophage T5 L-Shaped Tail Fibre with and without Its Intra-Molecular Chaperone" Viruses 7, no. 12: 6424-6440. https://doi.org/10.3390/v7122946

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

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