The NMR structure of the gpU tail-terminator protein from bacteriophage lambda: identification of sites contributing to Mg(II)-mediated oligomerization and biological function.

@article{Edmonds2007TheNS,
  title={The NMR structure of the gpU tail-terminator protein from bacteriophage lambda: identification of sites contributing to Mg(II)-mediated oligomerization and biological function.},
  author={Lizbeth Edmonds and Amanda Liu and Jamie Jun-Mae Kwan and Aida Avanessy and Mary Caracoglia and Irene Yang and Karen L Maxwell and John L R Rubenstein and Alan R. Davidson and Logan W Donaldson},
  journal={Journal of molecular biology},
  year={2007},
  volume={365 1},
  pages={175-86}
}
During the late stages of lambda bacteriophage assembly, the protein gpU terminates tail polymerization and participates at the interface between the mature capsid and tail components. When it engages the lambda tail, gpU undergoes a monomer-hexamer transition to achieve its biologically active form. Towards understanding how gpU participates in multiple protein-protein interactions, we have solved the structure of gpU in its monomeric state using NMR methods. The structure reveals a mixed… CONTINUE READING

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