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The solution structure of the bacteriophage lambda head-tail joining protein, gpFII.

Karen L Maxwell1, Adelinda A Yee, Cheryl H Arrowsmith

  • 1Department of Molecular and Medical Genetics, University of Toronto, Ont., Canada.

Journal of Molecular Biology
|June 27, 2002
PubMed
Summary

Bacteriophage lambda FII protein (gpFII) is essential for phage assembly. Biophysical and NMR studies reveal its novel structure, with unstructured regions potentially regulating head-tail joining.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Virology

Background:

  • The bacteriophage lambda FII protein (gpFII) is a critical structural component involved in phage morphogenesis.
  • gpFII facilitates the final step of phage assembly: the joining of heads and tails.

Purpose of the Study:

  • To characterize the biophysical properties and atomic structure of bacteriophage lambda gpFII.
  • To elucidate the role of gpFII's structure in phage assembly and identify potential binding surfaces.

Main Methods:

  • Biophysical experiments were conducted to assess gpFII stability, monomeric state, and folding reversibility.
  • Nuclear Magnetic Resonance (NMR) spectroscopy was employed to determine the atomic-resolution structure of gpFII.
  • Sequence alignment of gpFII with homologues from other lambdoid phages was performed.

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Main Results:

  • gpFII was found to be stable, monomeric, and reversibly folded.
  • The atomic structure revealed a novel fold comprising seven beta-strands and one alpha-helix.
  • Two significant unstructured regions were identified: residues 1-24 (N-terminus) and residues 46-62 (internal loop).
  • Sequence analysis allowed for the putative identification of surfaces mediating head and tail binding.

Conclusions:

  • The novel structure of gpFII, including its unstructured regions, likely plays a key role in regulating bacteriophage assembly.
  • Conformational changes in these unstructured regions during assembly are hypothesized to be important.
  • The identified binding surfaces provide insights into the molecular interactions governing phage head-tail joining.