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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Vydáno v:	Proc Natl Acad Sci U S A
Hlavní autoři:	Håkansson, Kjell, Wang, Andrew H.-J., Miller, Charles G.
Médium:	Artigo
Jazyk:	Inglês
Vydáno:	National Academy of Sciences 2000
Témata:	Biological Sciences
On-line přístup:	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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