Crystal structure of pb 9 , the distal tail protein of bacteriophage T 5 : A 1 conserved structural motif among all siphophages 2
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چکیده
5 Univ. Grenoble Alpes, Institut de Biologie Structurale (IBS), Grenoble, France. 6 CNRS, UMR5075, IBS, F-38027 Grenoble, France. 7 CEA, DSV, IBS, F-38027 Grenoble, France. 8 Max Planck Institute for Molecular Genetics, Berlin, Germany 9 Université de Lyon, Ecole Normale Supérieure de Lyon, Laboratoire de Chimie, UMR CNRS 5182, 10 Lyon, France. 11 Institut de Biochimie et de Biophysique Moléculaire et Cellulaire, Université Paris-Sud, UMR CNRS 12 8619, Orsay, France. 13 14 15 RUNNING TITLE: Structure of pb9, the Distal tail protein of phage T5 16
منابع مشابه
Crystal structure of pb9, the distal tail protein of bacteriophage T5: a conserved structural motif among all siphophages.
The tail of Caudovirales bacteriophages serves as an adsorption device, a host cell wall-perforating machine, and a genome delivery pathway. In Siphoviridae, the assembly of the long and flexible tail is a highly cooperative and regulated process that is initiated from the proteins forming the distal tail tip complex. In Gram-positive-bacterium-infecting siphophages, the distal tail (Dit) prote...
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تاریخ انتشار 2013