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      The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad.

      Proceedings of the National Academy of Sciences of the United States of America
      Catalytic Domain, Crystallography, X-Ray, Dipeptidases, chemistry, Glutamic Acid, Histidine, Models, Molecular, Protein Structure, Secondary, Salmonella typhimurium, enzymology, Serine

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          Abstract

          The three-dimensional structure of Salmonella typhimurium aspartyl dipeptidase, peptidase E, was solved crystallographically and refined to 1.2-A resolution. The structure of this 25-kDa enzyme consists of two mixed beta-sheets forming a V, flanked by six alpha-helices. The active site contains a Ser-His-Glu catalytic triad and is the first example of a serine peptidase/protease with a glutamate in the catalytic triad. The active site Ser is located on a strand-helix motif reminiscent of that found in alpha/beta-hydrolases, but the polypeptide fold and the organization of the catalytic triad differ from those of the known serine proteases. This enzyme is a member of a family of serine hydrolases and appears to represent a new example of convergent evolution of peptidase activity.

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          Author and article information

          Journal
          11106384
          18877
          10.1073/pnas.260376797

          Chemistry
          Catalytic Domain,Crystallography, X-Ray,Dipeptidases,chemistry,Glutamic Acid,Histidine,Models, Molecular,Protein Structure, Secondary,Salmonella typhimurium,enzymology,Serine

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