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- W2156427892 endingPage "661" @default.
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- W2156427892 abstract "A variety of proteins, including glycosylasparaginase, have recently been found to activate functions by self-catalyzed peptide bond rearrangements from single-chain precursors. Here we present the 1.9 A crystal structures of glycosylasparaginase precursors that are able to autoproteolyze via an N --> O acyl shift. Several conserved residues are aligned around the scissile peptide bond that is in a highly strained trans peptide bond configuration. The structure illustrates how a nucleophilic side chain may attack the scissile peptide bond at the immediate upstream backbone carbonyl and provides an understanding of the structural basis for peptide bond cleavage via an N --> O or N --> S acyl shift that is used by various groups of intramolecular autoprocessing proteins." @default.
- W2156427892 created "2016-06-24" @default.
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- W2156427892 date "1999-09-01" @default.
- W2156427892 modified "2023-10-16" @default.
- W2156427892 title "Structural Insights into the Mechanism of Intramolecular Proteolysis" @default.
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- W2156427892 doi "https://doi.org/10.1016/s0092-8674(00)80052-5" @default.
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