New insights into pb5, the receptor binding protein of bacteriophage T5, and its interaction with its Escherichia coli receptor FhuA
| Autor: | Maïté Paternostre, Pascale Boulanger, Frank Wien, Ali Flayhan, Cécile Breyton |
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| Přispěvatelé: | 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), Synchrotron SOLEIL (SSOLEIL), Centre National de la Recherche Scientifique (CNRS), Institut de Biologie et de Technologies de Saclay (IBITECS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay, Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Institut de biochimie et biophysique moléculaire et cellulaire (IBBMC), Université Paris-Sud - Paris 11 (UP11)-Centre National de la Recherche Scientifique (CNRS), 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) |
| Jazyk: | angličtina |
| Rok vydání: | 2012 |
| Předmět: |
[SDV]Life Sciences [q-bio]
medicine.disease_cause Biochemistry Protein Structure Secondary 03 medical and health sciences chemistry.chemical_compound Viral Proteins medicine Escherichia coli Bacteriophage T5 030304 developmental biology Ferrichrome [PHYS]Physics [physics] 0303 health sciences biology 030306 microbiology Protein Stability Binding protein Escherichia coli Proteins General Medicine biology.organism_classification Molecular biology Protein tertiary structure Cell biology chemistry Viral Receptor Proteolysis T-Phages Bacterial virus Bacterial outer membrane Bacterial Outer Membrane Proteins Protein Binding |
| Zdroj: | Biochimie Biochimie, Elsevier, 2012, 94 (9), pp.1982-1989. ⟨10.1016/j.biochi.2012.05.021⟩ Biochimie, 2012, 94 (9), pp.1982-1989. ⟨10.1016/j.biochi.2012.05.021⟩ |
| ISSN: | 0300-9084 |
| Popis: | International audience; The majority of bacterial viruses are bacteriophages bearing a tail that serves to recognise the bacterial surface and deliver the genome into the host cell. Infection is initiated by the irreversible interaction between the viral receptor binding protein (RBP) and a receptor at the surface of the bacterium. This interaction results ultimately in the phage DNA release in the host cytoplasm. Phage T5 infects Escher-ichia coli after binding of its RBP pb5 to the outer membrane ferrichrome transporter FhuA. Here, we have studied the complex formed by pb5 and FhuA by a variety of biophysical and biochemical techniques. We show that unlike RBPs of known structures, pb5 probably folds as a unique domain fulfilling both functions of binding to the host receptor and interaction with the rest of the phage. Pb5 likely binds to the domain occluding the b-barrel of FhuA as well as to external loops of the barrel. Furthermore, upon binding to FhuA, pb5 undergoes conformational changes, at the secondary and tertiary structure level that would be the key to the transmission of the signal through the tail to the capsid, triggering DNA release. This is the first structural information regarding the binding of a RBP to a proteic receptor. Ó 2012 Elsevier Masson SAS. All rights reserved. |
| Databáze: | OpenAIRE |
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