9gaf
PRECURSOR OF THE W11F MUTANT GLYCOSYLASPARAGINASE FROM FLAVOBACTERIUM MENINGOSEPTICUM
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OverviewOverview
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.
About this StructureAbout this Structure
9GAF is a Single protein structure of sequence from Elizabethkingia meningoseptica with GLY as ligand. Active as N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase, with EC number 3.5.1.26 Full crystallographic information is available from OCA.
ReferenceReference
Structural insights into the mechanism of intramolecular proteolysis., Xu Q, Buckley D, Guan C, Guo HC, Cell. 1999 Sep 3;98(5):651-61. PMID:10490104
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