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A Catalytic Ser–Lys Dyad in the Active Site of the ATP-Dependent Lon Protease from Escherichia coli

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Abstract

Two subfamilies of Lon proteases that differ in the structure of fragments containing the catalytically active Ser residue were revealed by the comparison of more than sixty sequences of Lon proteases from various sources. The absence of the classic catalytic triad in the active site of Lon proteases was confirmed. The catalytic site of Lon proteases was shown to be represented by the Ser–Lys dyad.

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Authors and Affiliations

  1. Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, GSP, Moscow, 117997, Russia

    T. V. Rotanova, E. E. Mel'nikov & K. B. Tsirulnikov

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  1. T. V. Rotanova
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  2. E. E. Mel'nikov
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  3. K. B. Tsirulnikov
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Rotanova, T.V., Mel'nikov, E.E. & Tsirulnikov, K.B. A Catalytic Ser–Lys Dyad in the Active Site of the ATP-Dependent Lon Protease from Escherichia coli . Russian Journal of Bioorganic Chemistry 29, 85–87 (2003). https://doi.org/10.1023/A:1022290705294

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