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Structure and Analysis of R1 and R2 Pyocin Receptor-Binding Fibers.

Sergey A Buth1, Mikhail M Shneider2,3, Dean Scholl4

  • 1Institute of Physics of Biologic Systems, École Polytechnique Fédérale de Lausanne (EPFL), BSP-415, 1015 Lausanne, Switzerland. sebuth@utmb.edu.

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Summary
This summary is machine-generated.

R-type pyocins are antibacterial proteins from Pseudomonas aeruginosa that kill other strains. Their tail fibers, crucial for target recognition and sheath contraction, have now had their crystal structures elucidated.

Keywords:
Pseudomonas aeruginosaR-type pyocinX-ray crystallographybacteriocincontractile injection systemsreceptor-binding protein

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Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • R-type pyocins are high-molecular weight bacteriocins produced by Pseudomonas aeruginosa.
  • They are structurally analogous to contractile bacteriophage tails.
  • Pyocins utilize tail fibers for target cell recognition and binding.

Purpose of the Study:

  • To determine the crystal structures of the C-terminal fragments of R1 and R2 pyocin fibers.
  • To elucidate the structural basis of receptor binding and sheath contraction triggering.

Main Methods:

  • X-ray crystallography was used to determine the structures of C-terminal fragments of R1 and R2 pyocin fibers.
  • Structural analysis focused on the receptor-binding domains and overall homotrimeric assembly.

Main Results:

  • The crystal structures reveal that both R1 and R2 pyocin fibers are homotrimers, approximately 240 Å long.
  • Each fiber comprises alternating rod-like and globular domains, including N-terminal knob domains and a C-terminal lectin-like domain.
  • Putative substrate binding sites are ~100 Å apart, suggesting a conformational change upon cell surface binding.

Conclusions:

  • The determined structures provide detailed insights into the architecture of pyocin tail fibers.
  • The findings suggest a mechanism where cell surface binding induces a conformational change, initiating sheath contraction for bacterial cell lysis.