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10.2217/fmb.14.91

http://scihub22266oqcxt.onion/10.2217/fmb.14.91
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suck abstract from ncbi


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pmid25517898
      Future+Microbiol 2014 ; 9 (12 ): 1319-27
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  • Structure and function of bacteriophage T4 #MMPMID25517898
  • Yap ML ; Rossmann MG
  • Future Microbiol 2014[]; 9 (12 ): 1319-27 PMID25517898 show ga
  • Bacteriophage T4 is the most well-studied member of Myoviridae, the most complex family of tailed phages. T4 assembly is divided into three independent pathways: the head, the tail and the long tail fibers. The prolate head encapsidates a 172 kbp concatemeric dsDNA genome. The 925 Å-long tail is surrounded by the contractile sheath and ends with a hexagonal baseplate. Six long tail fibers are attached to the baseplate's periphery and are the host cell's recognition sensors. The sheath and the baseplate undergo large conformational changes during infection. X-ray crystallography and cryo-electron microscopy have provided structural information on protein-protein and protein-nucleic acid interactions that regulate conformational changes during assembly and infection of Escherichia coli cells.
  • |Bacteriophage T4/genetics/*physiology/*ultrastructure [MESH]
  • |Cryoelectron Microscopy [MESH]
  • |Crystallography, X-Ray [MESH]
  • |Escherichia coli/*virology [MESH]
  • |Genome, Viral [MESH]
  • |Models, Molecular [MESH]
  • |Protein Conformation [MESH]
  • |Protein Structure, Tertiary [MESH]
  • |Viral Proteins/chemistry/genetics [MESH]


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