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Updated: Jun 5, 2026

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
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Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

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Crystal structure of the cytosolic Nudix-like domain of CD-NTase-associated protein 16 from Enterococcus faecalis

Tinashe Makanyire1, Zihan Zhou1, Wanqian Wu1

  • 1State Key Laboratory of Natural Medicines, School of Pharmacy, China Pharmaceutical University, Nanjing 211198, People's Republic of China.

Acta Crystallographica. Section F, Structural Biology Communications
|June 4, 2026
PubMed

Insights

Researchers elucidated the structure of a key bacterial defense protein, EfCap16, involved in cyclic oligonucleotide-based antiphage signaling systems (CBASS). This finding aids understanding of how bacteria combat phage infections.

Area of Science:

  • Structural biology
  • Microbiology
  • Molecular biology

Background:

  • Cyclic oligonucleotide-based antiphage signaling systems (CBASS) are crucial bacterial defense mechanisms against phages.
  • Membrane-associated CBASS effectors are vital but structurally undercharacterized.
  • Enterococcus faecalis CD-NTase-associated protein 16 (EfCap16) is a predicted CBASS effector with a transmembrane region and a Nudix-like domain.

Purpose of the Study:

  • To determine the crystal structure of the cytosolic Nudix domain of EfCap16.
  • To provide structural insights into transmembrane CBASS effectors.

Main Methods:

  • Recombinant expression and purification of the EfCap16 Nudix domain.
  • Crystallization and X-ray crystallography.
  • Structure determination at 1.6 Å resolution.

Main Results:

  • The crystal structure of the EfCap16 Nudix domain (PDB entry 22lg) was determined in space group P12₁1.
  • The structure reveals similarity to the Nudix superfamily, including a conserved Nudix motif.
  • The protein was purified to homogeneity and crystallized.

Conclusions:

  • The determined structure provides a foundational reference for EfCap16.
  • This structural information will facilitate future biochemical and functional studies of transmembrane CBASS effectors.
  • Understanding EfCap16 contributes to knowledge of bacterial antiphage defense systems.
Keywords:
CBASSNudix hydrolasestransmembrane effectors

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