Anna Sobiecka-Szkatula scite author profile

Background: An understanding of the HtrA protease activation mechanism is incomplete with respect to its LA regulatory loop.Results: A theoretical model of the LA structure is provided and experimentally verified. Conclusion: LA intersubunit contacts strongly contribute to the stabilization of the inactive HtrA. Significance: This is the first report that simultaneously offers a theoretical three-dimensional structure of LA and its biophysical and functional properties.

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Temperature-induced conformational changes within the regulatory loops L1–L2–LA of the HtrA heat-shock protease from Escherichia coli

Sobiecka-Szkatula

Polit

Scirè

et al. 2009

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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The proteolytic activity of the HtrA (DegP) protein from Escherichia coli at low temperatures

Skórko-Glonek

Sobiecka-Szkatula

Narkiewicz

et al. 2008

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Characterization of the chaperone-like activity of HtrA (DegP) protein from Escherichia coli under the conditions of heat shock

Skórko-Glonek

Laskowska

Sobiecka-Szkatula

et al. 2007

Archives of Biochemistry and Biophysics

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The role of the L2 loop in the regulation and maintaining the proteolytic activity of HtrA (DegP) protein from Escherichia coli

Sobiecka-Szkatula

Giełdoń

Scirè

et al. 2010

Archives of Biochemistry and Biophysics

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