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A bacterial surface layer protein exploits multistep crystallization for rapid self-assembly.

Jonathan Herrmann1,2, Po-Nan Li2,3, Fatemeh Jabbarpour1,2

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Surface layers (S-layers) are protein coats on microbes that self-assemble. A new study reveals a calcium-triggered pathway where a nucleation domain dramatically speeds up crystallization for S-layer proteins (SLPs).

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Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Surface layers (S-layers) are crystalline protein envelopes found on many microorganisms.
  • S-layer proteins (SLPs) self-assemble into 2D lattices upon environmental triggers.
  • The precise molecular mechanisms driving rapid S-layer protein crystallization are not fully understood.

Purpose of the Study:

  • To elucidate the molecular mechanisms behind the rapid in vitro crystallization of Caulobacter crescentus S-layer protein (SLP).
  • To investigate the role of different protein domains in the calcium-triggered assembly pathway.

Main Methods:

  • Utilized time-course electron cryo-microscopy (Cryo-EM) to observe the crystallization process.
  • Analyzed the distinct functions of the N-terminal nucleation domain and C-terminal crystallization domain.

Main Results:

  • Demonstrated a calcium-triggered, multistep assembly pathway for C. crescentus SLP crystallization into sheets.
  • Identified a nucleation domain that significantly accelerates crystallization compared to the lattice-forming domain alone.
  • Observed a crystalline intermediate with dynamic N-terminal domains, facilitating nucleation on curved surfaces.

Conclusions:

  • The N-terminal nucleation domain is critical for rapid S-layer assembly, enhancing kinetics.
  • Dynamic flexibility between domains explains efficient nucleation on microbial cell surfaces.
  • Findings suggest potential for engineering kinetically controlled self-assembling 2D nanomaterials.