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Protein degradation

Fits like a glove

Nature Reviews Molecular Cell Biology volume 10, page 4 (2009)Cite this article

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The highly conserved 'N-end rule pathway' selects proteins for degradation on the basis of the identity of their amino terminal residue. In bacteria, the adaptor protein ClpS recognizes N-end rule substrates and transfers them to the ATP-dependent Clp protease complex (ClpAP) for degradation.

Baker and colleagues determined the 1.15 Å crystal structure of ClpS in complex with a mimic peptide that contained an N-terminal Tyr, which is one of the universally recognized N-end rule residues. They found that the Tyr side chain 'fits like a glove' into a deep hydrophobic pocket on the surface of ClpS, and also found that the target peptide α-amino group forms hydrogen bonds with ClpS side chains at the entrance to the pocket.

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References

ORIGINAL RESEARCH PAPER

  1. Wang, K. H. et al. The molecular basis of N-end rule recognition. Mol. Cell 32, 406–414 (2008)

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FURTHER READING

  1. Ravid, T. & Hochstrasser, M. Diversity of degradation signals in the ubiquitin–proteasome system. Nature Rev. Mol. Cell Biol. 9, 679–689 (2008)

    Article  CAS  Google Scholar 

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Authors
  1. Francesca Cesari
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Cesari, F. Fits like a glove. Nat Rev Mol Cell Biol 10, 4 (2009). https://doi.org/10.1038/nrm2601

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