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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...
Gorde:
| Egile Nagusiak: | , , |
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| Formatua: | Artigo |
| Hizkuntza: | Inglês |
| Argitaratua: |
The National Academy of Sciences
2000
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| Gaiak: | |
| Sarrera elektronikoa: | https://ncbi.nlm.nih.gov/pmc/articles/PMC18877/ https://ncbi.nlm.nih.gov/pubmed/11106384 |
| Etiketak: |
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