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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| Gepubliceerd in: | Proc Natl Acad Sci U S A |
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| Hoofdauteurs: | , , |
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
National Academy of Sciences
2000
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC18877/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/11106384/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.260376797 |
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