9GAC

PRECURSOR OF THE T152C MUTANT GLYCOSYLASPARAGINASE FROM FLAVOBACTERIUM MENINGOSEPTICUM

Summary for 9GAC

• Entry DOI: 10.2210/pdb9gac/pdb
• Descriptor: PROTEIN (GLYCOSYLASPARAGINASE), GLYCINE (3 entities in total)
• Functional Keywords: precursor, glycosylasparaginase, n-terminal nucleophile, autoproteolysis, mutant, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Elizabethkingia meningoseptica
• Cellular location: Periplasm: Q47898
• Total number of polymer chains: 2
• Total formula weight: 64513.48

Authors

Guo, H.-C.,Xu, Q. (deposition date: 1999-06-15, release date: 2000-06-16, Last modification date: 2023-09-20)

Primary citation

Xu, Q.,Buckley, D.,Guan, C.,Guo, H.C.
Structural insights into the mechanism of intramolecular proteolysis.
Cell(Cambridge,Mass.), 98:651-661, 1999

PubMed 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.

PubMed: 10490104
DOI: 10.1016/S0092-8674(00)80052-5

Experimental method

X-RAY DIFFRACTION (1.9 Å)