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The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad
The three-dimensional structure of Salmonella typhimurium aspartyl dipeptidase, peptidase E, was solved crystallographically and refined to 1.2-Å resolution. The structure of this 25-kDa enzyme consists of two mixed β-sheets forming a V, flanked by six α-helices. The active site contains a Ser-His-G...
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| Auteurs principaux: | , , |
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| Format: | Artigo |
| Langue: | Inglês |
| Publié: |
The National Academy of Sciences
2000
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| Sujets: | |
| Accès en ligne: | https://ncbi.nlm.nih.gov/pmc/articles/PMC18877/ https://ncbi.nlm.nih.gov/pubmed/11106384 |
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