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Metalloenzymes

Cage redesign explains assembly

Nature Chemical Biology volume 9, pages 143144 (2013) | Download Citation

Control of protein self-assembly and disassembly, which is central to metabolism and engineering applications, remains challenging. Here, a perspicacious redesign of interfaces in the multisubunit ferritin protein cage provides single, modifiable subunits that assemble with Cu2+ templating and give insights into the cage assembly code.

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References

  1. 1.

    & Science 312, 873–875 (2006).

  2. 2.

    et al. Science 319, 1083–1086 (2008).

  3. 3.

    Curr. Opin. Chem. Biol. 15, 304–311 (2011).

  4. 4.

    , & Nat. Chem. Biol. 9, 169–176 (2013).

  5. 5.

    et al. Chem. Commun. (Camb.) 47, 3475–3477 (2011).

  6. 6.

    et al. Biomaterials 32, 1430–1437 (2011).

  7. 7.

    , , , & J. Am. Chem. Soc. 132, 14562–14569 (2010).

  8. 8.

    , , , & Proc. Natl. Acad. Sci. USA 107, 545–550 (2010).

  9. 9.

    et al. J. Am. Chem. Soc. 134, 6169–6176 (2012).

Download references

Author information

Affiliations

  1. Elizabeth C. Theil is at the Children's Hospital Oakland Research Institute, Oakland, California, USA, and the Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, North Carolina, USA.

    • Elizabeth C Theil
  2. Paola Turano is at the Magnetic Resonance Center (CERM), University of Florence, Florence, Italy, and the Department of Chemistry, University of Florence, Florence, Italy.

    • Paola Turano

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Competing interests

The authors declare no competing financial interests.

Corresponding authors

Correspondence to Elizabeth C Theil or Paola Turano.

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DOI

https://doi.org/10.1038/nchembio.1182

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