title: Assessing the conformational changes of pb5, the receptor-binding protein of phage T5, upon binding to its Escherichia coli receptor FhuA.
abstract: Within tailed bacteriophages, interaction of the receptor-binding protein (RBP) with the target cell triggers viral DNA ejection into the host cytoplasm. In the case of phage T5, the RBP pb5 and the receptor FhuA, an outer membrane protein of Escherichia coli, have been identified. Here, we use small angle neutron scattering and electron microscopy to investigate the FhuA-pb5 complex. Specific deuteration of one of the partners allows the complete masking in small angle neutron scattering of the surfactant and unlabeled proteins when the complex is solubilized in the fluorinated surfactant F6-DigluM. Thus, individual structures within a membrane protein complex can be described. The solution structure of FhuA agrees with its crystal structure; that of pb5 shows an elongated shape. Neither displays significant conformational changes upon interaction. The mechanism of signal transduction within phage T5 thus appears different from that of phages binding cell wall saccharides, for which structural information is available.
authors.affiliation: From the Université Grenoble Alpes, Institut de Biologie Structurale (IBS), F-38027 Grenoble, France,; CNRS, UMR5075, IBS, F-38027 Grenoble, France,; the Commissariat à l'Energie Atomique, DSV, IBS, F-38027 Grenoble, France,. Electronic address: Cecile.Breyton@ibs.fr.
authors.forename: Cécile
authors.initials: C
authors.lastname: Breyton
authors.affiliation: From the Université Grenoble Alpes, Institut de Biologie Structurale (IBS), F-38027 Grenoble, France,; CNRS, UMR5075, IBS, F-38027 Grenoble, France,; the Commissariat à l'Energie Atomique, DSV, IBS, F-38027 Grenoble, France.
authors.forename: Ali
authors.initials: A
authors.lastname: Flayhan
authors.affiliation: From the Université Grenoble Alpes, Institut de Biologie Structurale (IBS), F-38027 Grenoble, France,; CNRS, UMR5075, IBS, F-38027 Grenoble, France,; the Commissariat à l'Energie Atomique, DSV, IBS, F-38027 Grenoble, France.
authors.forename: Frank
authors.initials: F
authors.lastname: Gabel
authors.affiliation: From the Université Grenoble Alpes, Institut de Biologie Structurale (IBS), F-38027 Grenoble, France,; CNRS, UMR5075, IBS, F-38027 Grenoble, France,; the Commissariat à l'Energie Atomique, DSV, IBS, F-38027 Grenoble, France.
authors.forename: Mathilde
authors.initials: M
authors.lastname: Lethier
authors.affiliation: the Université d'Avignon, Equipe Chimie Bioorganique et Systèmes Amphiphiles, F-84029 Avignon, France,; the Institut des Biomolécules Max Mousseron, UMR 5247, F-34093 Montpellier, France.
authors.forename: Grégory
authors.initials: G
authors.lastname: Durand
authors.affiliation: the Institut de Biochimie et de Biophysique Moléculaire et Cellulaire, Université Paris-Sud, UMR CNRS 8619, F-91405 Orsay, France, and.
authors.forename: Pascale
authors.initials: P
authors.lastname: Boulanger
authors.affiliation: the Center for Cellular Imaging and NanoAnalytics, Biozentrum, University Basel, CH-4058 Basel, Switzerland.
authors.forename: Mohamed
authors.initials: M
authors.lastname: Chami
authors.affiliation: From the Université Grenoble Alpes, Institut de Biologie Structurale (IBS), F-38027 Grenoble, France,; CNRS, UMR5075, IBS, F-38027 Grenoble, France,; the Commissariat à l'Energie Atomique, DSV, IBS, F-38027 Grenoble, France.
authors.forename: Christine
authors.initials: C
authors.lastname: Ebel
mesh_terms: D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D004926:Escherichia coli / Q000737:chemistry* / Q000378:metabolism / Q000821:virology; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism; D046912:Multiprotein Complexes / Q000737:chemistry* / Q000378:metabolism; D033363:Neutron Diffraction; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D053838:Scattering, Small Angle; D017906:Siphoviridae / Q000737:chemistry* / Q000378:metabolism; D013501:Surface-Active Agents; D015678:Viral Structural Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D001425:Bacterial Outer Membrane Proteins; D029968:Escherichia coli Proteins; C050900:FhuA protein, E coli; D046912:Multiprotein Complexes; D013501:Surface-Active Agents; D015678:Viral Structural Proteins
keywords: Bacteriophage; Biophysics; Electron Microscopy (EM); Fluorinated Surfactant; Membrane Proteins; Small Angle Neutron Scattering; Viral Protein