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5 results on '"MESH: Siphoviridae"'

1. Structural basis of bacteriophage T5 infection trigger and E. coli cell wall perforation

Author

Romain Linares, Charles-Adrien Arnaud, Grégory Effantin, Claudine Darnault, Nathan Hugo Epalle, Elisabetta Boeri Erba, Guy Schoehn, Cécile Breyton, Institut de biologie structurale (IBS - UMR 5075), Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA), Groupe Membrane et pathogènes (IBS-MP), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Cryo-EM, spectro de masse, Grenoble Instruct-ERIC Center (ISBG, UAR 3518 CNRS-CEA-UGA-EMBL), Grenoble Partnership for Structural Biology (PSB), University Grenoble Alpes graduate school (Ecoles Universitaires de Recherche), Auvergne-Rhône- Alpes Region, Fondation pour la Recherche Médicale (FRM), Fonds FEDER, GIS-Infrastructures en Biologie Santé et Agronomie (IBiSA), ANR-16-CE11-0027,PerfoBac,Comment les bactériophages perforent-ils la paroi des bactéries ?(2016), ANR-21-CE11-0023,Schizoceptor,Structure et impact des lipides sur l'heteromer 5-HT2A-mGlu2, cible pharmacologique de la schizophrénie(2021), ANR-10-INBS-0005,FRISBI,Infrastructure Française pour la Biologie Structurale Intégrée(2010), and ANR-17-EURE-0003,CBH-EUR-GS,CBH-EUR-GS(2017)

Subjects
Multidisciplinary, MESH: Cell Wall, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], MESH: Escherichia coli, [SDV]Life Sciences [q-bio], [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology, MESH: Siphoviridae, MESH: Bacteriophages, MESH: Cryoelectron Microscopy
Abstract

The vast majority of bacteriophages (phages) - bacterial viruses - present a tail that allows host recognition, cell wall perforation and safe channelling of the viral DNA from the capsid to the cytoplasm of the infected bacterium. The majority of tailed phages bears a long flexible tail (Siphoviridae) at the distal end of which a tip complex, often called baseplate, harbours one or more Receptor Binding Protein·s (RBPs). Interaction between the RBPs and the host surface triggers cell wall perforation and DNA ejection, but little is known on these mechanisms for Siphoviridae. Here, we present the structure of siphophage T5 tip at high resolution, determined by electron cryo-microscopy, allowing to trace most of its constituting proteins, including 35 C-terminal residues of the Tape Measure Protein. We also present the structure of T5 tip after interaction with its E. coli receptor FhuA reconstituted into nanodisc. It brings out the dramatic conformational changes underwent by T5 tip upon infection, i.e. bending of the central fibre on the side, opening of the tail tube and its anchoring to the membrane, and formation of a transmembrane channel. These new structures shed light on the mechanisms of host recognition and activation of the viral entry for Siphoviridae.

Published
2022
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2. Characterization of a triad of genes in cyanophage S-2L sufficient to replace adenine by 2-aminoadenine in bacterial DNA

Author

Dariusz Czernecki, Frédéric Bonhomme, Pierre-Alexandre Kaminski, Marc Delarue, Architecture et Dynamique des Macromolécules Biologiques - Architecture and Dynamics of Biological Macromolecules, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Collège doctoral [Sorbonne universités], Sorbonne Université (SU), Chimie biologique épigénétique - Epigenetic Chemical Biology (EpiCBio), Biologie des Bactéries pathogènes à Gram-positif - Biology of Gram-Positive Pathogens, The authors acknowledge a DIM1Health 2019 grant from the Région Ile de France to the project EpiK (coordinated by P.B. Arimondo) for the LCMS equipment., We thank the Crystallogenesis and Crystallography Platform (PF6) of Institut Pasteur for help in crystallization and preliminary crystallographic data collection. We thank Marcel Hollenstein and his group for the use of their HPLC system. We also thank staff from PROXIMA−1 and PROXIMA-2 beamlines for help in data collection and SOLEIL (Saint-Aubin, France) and for provision of synchrotron radiation facilities. We thank Pierre Legrand for discussions regarding the structural aspect of this work, as well as Laurent Debarbieux and his group for discussions regarding phages. We also thank Stéphane Decorps-Declere from the Hub de Bioinformatique et Biostatistique (C3BI, Institut Pasteur) for help with the S-2L genome mapping and its deposition., Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité), Collège Doctoral, Université Paris Cité (UPCité)-Microbiologie Intégrative et Moléculaire (UMR6047), and Institut Pasteur [Paris] (IP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut Pasteur [Paris] (IP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)

Subjects
DNA, Bacterial, Models, Molecular, Genes, Viral, Protein Conformation, Science, Static Electricity, MESH: Base Pairing, Genome, Viral, Siphoviridae, Crystallography, X-Ray, Article, MESH: Recombinant Proteins, Adenylosuccinate Synthase, Viral Proteins, MESH: Protein Conformation, Escherichia coli, DNA metabolism, MESH: 2-Aminopurine, Bacteriophages, MESH: Adenylosuccinate Synthase, MESH: Siphoviridae, MESH: Bacteriophages, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], 2-Aminopurine, Base Pairing, MESH: Static Electricity, X-ray crystallography, MESH: Genes, Viral, Deoxyadenosines, MESH: Escherichia coli, MESH: Podoviridae, MESH: Deoxyadenosines, Podoviridae, MESH: Crystallography, X-Ray, MESH: Viral Proteins, MESH: DNA, Bacterial, Phosphoric Monoester Hydrolases, Recombinant Proteins, MESH: DNA, Viral, MESH: Metabolic Networks and Pathways, DNA, Viral, MESH: Phosphoric Monoester Hydrolases, MESH: Genome, Viral, Structural biology, Metabolic Networks and Pathways, MESH: Models, Molecular
Abstract

Cyanophage S-2L is known to profoundly alter the biophysical properties of its DNA by replacing all adenines (A) with 2-aminoadenines (Z), which still pair with thymines but with a triple hydrogen bond. It was recently demonstrated that a homologue of adenylosuccinate synthetase (PurZ) and a dATP triphosphohydrolase (DatZ) are two important pieces of the metabolism of 2-aminoadenine, participating in the synthesis of ZTGC-DNA. Here, we determine that S-2L PurZ can use either dATP or ATP as a source of energy, thereby also depleting the pool of nucleotides in dATP. Furthermore, we identify a conserved gene (mazZ) located between purZ and datZ genes in S-2L and related phage genomes. We show that it encodes a (d)GTP-specific diphosphohydrolase, thereby providing the substrate of PurZ in the 2-aminoadenine synthesis pathway. High-resolution crystal structures of S-2L PurZ and MazZ with their respective substrates provide a rationale for their specificities. The Z-cluster made of these three genes – datZ, mazZ and purZ – was expressed in E. coli, resulting in a successful incorporation of 2-aminoadenine in the bacterial chromosomal and plasmidic DNA. This work opens the possibility to study synthetic organisms containing ZTGC-DNA., The cyanophage S-2L incorporates 2-aminoadenine (Z) instead of adenine into its DNA, which still pairs with thymine forming a triple hydrogen bond. Here, the authors identify a third gene mazZ located between purZ and datZ that is required for 2-aminoadenine biosynthesis and determine the crystal structures of MazZ and PurZ. They further show that co-expression of these three genes in E.coli enables 2-aminoadenine incorporation into the bacterial genome.

Published
2021
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3. Noncanonical DNA polymerization by aminoadenine-based siphoviruses

Author

Faten Jaziri, Philippe Marliere, Dominique Louis, Sylvie Pochet, Graham F. Hatfull, Jef Rozenski, Pierre-Yves Bourguignon, Piet Herdewijn, Deborah Jacobs-Sera, Pierre-Alexandre Kaminski, Valérie Pezo, Génomique métabolique (UMR 8030), Genoscope - Centre national de séquençage [Evry] (GENOSCOPE), Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université d'Évry-Val-d'Essonne (UEVE), Werkstatt fuer Potenzielle Genetik [Berlin], TESSI [Paris], Alderys [Orsay], University of Pittsburgh (PITT), Pennsylvania Commonwealth System of Higher Education (PCSHE), Rega Institute for Medical Research [Leuven, België], Catholic University of Leuven - Katholieke Universiteit Leuven (KU Leuven), Chimie organique (CNR - UMR3523), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut Pasteur [Paris], Biologie des Bactéries pathogènes à Gram-positif, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), The research received funding from the European Research Council (ERC-2012-ADG-20120216/320683) and from the European Commission (ERASynBio BB/ N01023X/1 and ANR-15-SYNB-0003-04)., ANR-15-SYNB-0003,invivoXNA,Orthogonal biosystems based on phosphonate XNAs(2015), European Project: 320683,EC:FP7:ERC,ERC-2012-ADG_20120216,XNA(2013), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université d'Évry-Val-d'Essonne (UEVE)-Centre National de la Recherche Scientifique (CNRS), Chimie organique (CNRS - UMR3523), Institut Pasteur [Paris] (IP)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), and Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS)

Subjects
0301 basic medicine, Exonuclease, DNA Replication, DNA polymerase, MESH: DNA Replication, DNA-Directed DNA Polymerase, Genome, Viral, Siphoviridae, Viral Nonstructural Proteins, 010402 general chemistry, 01 natural sciences, Polymerization, 03 medical and health sciences, chemistry.chemical_compound, MESH: DNA-Directed DNA Polymerase, MESH: 2-Aminopurine, MESH: Siphoviridae, 2-Aminopurine, MESH: Phylogeny, Polymerase, Phylogeny, Klenow fragment, Multidisciplinary, biology, Chemistry, DNA replication, [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, 0104 chemical sciences, Thymine, MESH: DNA, Viral, 030104 developmental biology, MESH: Polymerization, Biochemistry, DNA, Viral, biology.protein, MESH: Viral Nonstructural Proteins, DNA polymerase I, MESH: Genome, Viral, DNA
Abstract

Biosynthesis and replication, from A to Z Four nucleobases. adenine (A), cytosine (C), guanine (G), and thymine (T), are usually thought to be invariable in DNA. In bacterial viruses, however, each of the DNA bases have variations that help them to escape degradation by bacterial restriction enzymes. In the genome of cyanophage S-2L, A is completely replaced by diaminopurine (Z), which forms three hydrogen bonds with T and thus creates non–Watson-Crick base pairing in the DNA of this virus (see the Perspective by Grome and Isaacs). Zhou et al. and Sleiman et al. determined the biochemical pathway that produces Z, which revealed more Z genomes in viruses hosted in bacteria distributed widely in the environment and phylogeny. Pezo et al. identified a DNA polymerase that incorporates Z into DNA while rejecting A. These findings enrich our understanding of biodiversity and expand the genetic palette for synthetic biology. Science , this issue p. 512 , 516 , 520 ; see also p. 460

Published
2021
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4. Insights into bacteriophage T5 structure from analysis of its morphogenesis genes and protein components

Author

Luc Ponchon, Alexis Huet, Madalena Renouard, Cécile Breyton, Rudi Lurz, Pascale Boulanger, Fabrice Confalonieri, Alan R. Davidson, Mohamed Chami, Yvan Zivanovic, Ali Flayhan, Paulette Decottignies, Institut de génétique et microbiologie [Orsay] (IGM), Université Paris-Sud - Paris 11 (UP11)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de cristallographie et RMN biologiques (LCRB - UMR 8015), Université Paris Descartes - Paris 5 (UPD5)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Centre d'études et de recherche en informatique et communications (CEDRIC), Ecole Nationale Supérieure d'Informatique pour l'Industrie et l'Entreprise (ENSIIE)-Conservatoire National des Arts et Métiers [CNAM] (CNAM), Institut de biologie structurale (IBS - UMR 5075 ), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Laboratoire pour l'utilisation du rayonnement électromagnétique (LURE), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-MENRT-Centre National de la Recherche Scientifique (CNRS), Muséum national d'Histoire naturelle (MNHN), Institut de biochimie et biophysique moléculaire et cellulaire (IBBMC), Laboratoire de Réactivité de Surface (LRS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), HESAM Université - Communauté d'universités et d'établissements Hautes écoles Sorbonne Arts et métiers université (HESAM)-HESAM Université - Communauté d'universités et d'établissements Hautes écoles Sorbonne Arts et métiers université (HESAM), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5), Institut de biologie structurale (IBS - UMR 5075), Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC), Institut de génétique et microbiologie [Orsay] ( IGM ), Université Paris-Sud - Paris 11 ( UP11 ) -Centre National de la Recherche Scientifique ( CNRS ), Laboratoire de cristallographie et RMN biologiques ( LCRB - UMR 8015 ), Université Paris Descartes - Paris 5 ( UPD5 ) -Centre National de la Recherche Scientifique ( CNRS ), Centre d'étude et de recherche en informatique et communications ( CEDRIC ), Ecole Nationale Supérieure d'Informatique pour l'Industrie et l'Entreprise ( ENSIIE ) -Conservatoire National des Arts et Métiers [CNAM] ( CNAM ), Institut de biologie structurale ( IBS - UMR 5075 ), Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Centre National de la Recherche Scientifique ( CNRS ) -Université Grenoble Alpes ( UGA ) -Université Joseph Fourier - Grenoble 1 ( UJF ), Laboratoire pour l'utilisation du rayonnement électromagnétique ( LURE ), Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -MENRT-Centre National de la Recherche Scientifique ( CNRS ), Muséum National d'Histoire Naturelle ( MNHN ), Institut de biochimie et biophysique moléculaire et cellulaire ( IBBMC ), Laboratoire de Réactivité de Surface ( LRS ), and Université Pierre et Marie Curie - Paris 6 ( UPMC ) -Centre National de la Recherche Scientifique ( CNRS )

Subjects
MESH : Escherichia coli, MESH : Molecular Sequence Data, viruses, MESH: Amino Acid Sequence, Siphoviridae, Genome, chemistry.chemical_compound, MESH: Capsid, Bacteriophages, MESH : Viral Proteins, Bacteriophage T5, MESH : Siphoviridae, 0303 health sciences, biology, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], MESH: Escherichia coli, MESH : Amino Acid Sequence, MESH : Sequence Alignment, 030302 biochemistry & molecular biology, MESH : Bacteriophages, Cell biology, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Capsid, Lytic cycle, MESH : Capsid, Molecular Sequence Data, Immunology, MESH: Sequence Alignment, MESH: Microscopy, Electron, Microbiology, Viral Proteins, 03 medical and health sciences, Virology, Escherichia coli, MESH: Siphoviridae, Amino Acid Sequence, MESH: Bacteriophages, Gene, 030304 developmental biology, MESH: Molecular Sequence Data, Structure and Assembly, biology.organism_classification, Molecular biology, MESH: Viral Proteins, MESH : Microscopy, Electron, Microscopy, Electron, chemistry, Cytoplasm, Insect Science, Sequence Alignment, DNA, [ SDV.BBM.BS ] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM]
Abstract

Bacteriophage T5 represents a large family of lytic Siphoviridae infecting Gram-negative bacteria. The low-resolution structure of T5 showed the T=13 geometry of the capsid and the unusual trimeric organization of the tail tube, and the assembly pathway of the capsid was established. Although major structural proteins of T5 have been identified in these studies, most of the genes encoding the morphogenesis proteins remained to be identified. Here, we combine a proteomic analysis of T5 particles with a bioinformatic study and electron microscopic immunolocalization to assign function to the genes encoding the structural proteins, the packaging proteins, and other nonstructural components required for T5 assembly. A head maturation protease that likely accounts for the cleavage of the different capsid proteins is identified. Two other proteins involved in capsid maturation add originality to the T5 capsid assembly mechanism: the single head-to-tail joining protein, which closes the T5 capsid after DNA packaging, and the nicking endonuclease responsible for the single-strand interruptions in the T5 genome. We localize most of the tail proteins that were hitherto uncharacterized and provide a detailed description of the tail tip composition. Our findings highlight novel variations of viral assembly strategies and of virion particle architecture. They further recommend T5 for exploring phage structure and assembly and for deciphering conformational rearrangements that accompany DNA transfer from the capsid to the host cytoplasm.

Published
2014
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5. Assessing the conformational changes of pb5, the receptor-binding protein of phage T5, upon binding to its Escherichia coli receptor FhuA

Author

Mohamed Chami, Frank Gabel, Mathilde Lethier, Pascale Boulanger, Cécile Breyton, Christine Ebel, Grégory Durand, Ali Flayhan, Institut de biologie structurale (IBS - UMR 5075 ), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] (IBMM), Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM)-Institut de Chimie du CNRS (INC)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Avignon Université (AU), Institut de biochimie et biophysique moléculaire et cellulaire (IBBMC), Université Paris-Sud - Paris 11 (UP11)-Centre National de la Recherche Scientifique (CNRS), University of Basel (Unibas), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), and Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG)

Subjects
MESH: Protein Structure, Quaternary, Viral protein, viruses, MESH: Escherichia coli Proteins, MESH: Viral Structural Proteins, Biology, Siphoviridae, medicine.disease_cause, Biochemistry, Bacteriophage, 03 medical and health sciences, Surface-Active Agents, MESH: Protein Structure, Tertiary, Scattering, Small Angle, medicine, Escherichia coli, MESH: Siphoviridae, Protein Structure, Quaternary, Molecular Biology, MESH: Scattering, Small Angle, 030304 developmental biology, Viral Structural Proteins, 0303 health sciences, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], MESH: Escherichia coli, Escherichia coli Proteins, 030302 biochemistry & molecular biology, MESH: Bacterial Outer Membrane Proteins, MESH: Surface-Active Agents, Cell Biology, MESH: Multiprotein Complexes, biology.organism_classification, Protein Structure, Tertiary, MESH: Neutron Diffraction, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Neutron Diffraction, Membrane protein, Membrane protein complex, Cytoplasm, Multiprotein Complexes, Biophysics, Signal transduction, Bacterial outer membrane, Molecular Biophysics, Bacterial Outer Membrane Proteins
Abstract

International audience; 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.

Published
2013
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