3LJQ

Crystal Structure of the Glycosylasparaginase T152C apo-precursor

Summary for 3LJQ

• Entry DOI: 10.2210/pdb3ljq/pdb
• Related: 1P4K 1P4V 9GAA 9GAC 9GAF
• Descriptor: N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase, SODIUM ION, GLYCINE, ... (4 entities in total)
• Functional Keywords: aspartylglucosylaminase, active precursors, precursor structure, reversible inhibitor, constrained conformation, autoproteolysis, catalytic mechanism, n-terminal nucleophile hydrolases, hydrolase
• Biological source: Flavobacterium meningosepticum
• Cellular location: Periplasm: Q47898
• Total number of polymer chains: 2
• Total formula weight: 65285.15

Authors

Wang, Y.,Guo, H.-C. (deposition date: 2010-01-26, release date: 2010-11-24, Last modification date: 2023-09-06)

Primary citation

Wang, Y.,Guo, H.C.
Crystallographic snapshot of glycosylasparaginase precursor poised for autoprocessing.
J.Mol.Biol., 403:120-130, 2010

PubMed Abstract: Glycosylasparaginase belongs to a family of N-terminal nucleophile hydrolases that autoproteolytically generate their mature enzymes from single-chain protein precursors. Previously, based on a precursor structure paused at pre-autoproteolysis stage by a reversible inhibitor (glycine), we proposed a mechanism of intramolecular autoproteolysis. A key structural feature, a highly strained conformation at the scissile peptide bond, had been identified and was hypothesized to be critical for driving autoproteolysis through an N-O acyl shift. To examine this "twist-and-break" hypothesis, we report here a 1. 9-Å-resolution structure of an autoproteolysis-active precursor (a T152C mutant) that is free of inhibitor or ligand and is poised to undergo autoproteolysis. The current crystallographic study has provided direct evidence for the natural conformation of the glycosylasparaginase autocatalytic site without influence from any inhibitor or ligand. This finding has confirmed our previous proposal that conformational strain is an intrinsic feature of an active precursor.

PubMed: 20800597
DOI: 10.1016/j.jmb.2010.08.038

Experimental method

X-RAY DIFFRACTION (1.9 Å)