A conserved activation cluster is required for allosteric communication in HtrA-family proteases.

@article{Regt2015ACA,
  title={A conserved activation cluster is required for allosteric communication in HtrA-family proteases.},
  author={Anna K de Regt and Seokhee Kim and Jungsan Sohn and Robert A. Grant and Tania A. Baker and Robert T. Sauer},
  journal={Structure},
  year={2015},
  volume={23 3},
  pages={517-526}
}
In E. coli, outer-membrane stress causes a transcriptional response through a signaling cascade initiated by DegS cleavage of a transmembrane antisigma factor. Each subunit of DegS, an HtrA-family protease, contains a protease domain and a PDZ domain. The trimeric protease domain is autoinhibited by the unliganded PDZ domains. Allosteric activation requires binding of unassembled outer-membrane proteins (OMPs) to the PDZ domains and protein substrate binding. Here, we identify a set of DegS… CONTINUE READING

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Proceedings of the National Academy of Sciences of the United States of America • 2015

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