Related Experiment Video
Updated: Aug 12, 2026

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
Published on: July 5, 2018
Crystal structure of glycosylasparaginase from Flavobacterium meningosepticum
J Xuan1, A L Tarentino, B G Grimwood
1Division of Molecular Medicine, Wadsworth Center, New York State Department of Health, Albany 12201, USA.
Abstract:
The crystal structure of recombinant glycosylasparaginase from Flavobacterium meningosepticum has been determined at 2.32 angstroms resolution. This enzyme is a glycoamidase that cleaves the link between the asparagine and the N-acetylglucosamine of N-linked oligosaccharides and plays a major role in the degradation of glycoproteins. The three-dimensional structure of the bacterial enzyme is very similar to that of the human enzyme, although it lacks the four disulfide bridges found in the human enzyme. The main difference is the absence of a small random coil domain at the end of the alpha-chain that forms part of the substrate binding cleft and that has a role in the stabilization of the tetramer of the human enzyme. The bacterial glycosylasparaginase is observed as an (alphabeta)2-tetramer in the crystal, despite being a dimer in solution. The study of the structure of the bacterial enzyme allows further evaluation of the effects of disease-causing mutations in the human enzyme and confirms the suitability of the bacterial enzyme as a model for functional analysis.
Insights
The crystal structure of bacterial glycosylasparaginase reveals similarities to the human enzyme but lacks disulfide bridges. This bacterial enzyme serves as a valuable model for studying human glycosylasparaginase and related diseases.
Area of Science:
- Biochemistry
- Structural Biology
- Enzymology
Background:
- Glycosylasparaginase is a key enzyme in glycoprotein degradation, cleaving asparagine-N-acetylglucosamine bonds in N-linked oligosaccharides.
- Understanding enzyme structure is crucial for elucidating function and disease mechanisms.
Purpose of the Study:
- To determine the crystal structure of recombinant glycosylasparaginase from Flavobacterium meningosepticum.
- To compare the structural features of the bacterial enzyme with its human counterpart.
- To assess the utility of the bacterial enzyme as a model for functional studies.
Main Methods:
- X-ray crystallography was employed to determine the enzyme's three-dimensional structure.
- The crystal structure was resolved at a resolution of 2.32 angstroms.
Main Results:
- The crystal structure of bacterial glycosylasparaginase was elucidated, revealing significant structural homology to the human enzyme.
- Key differences include the absence of four disulfide bridges and a specific random coil domain in the bacterial enzyme.
- The bacterial enzyme forms an (alphabeta)2-tetramer in the crystal, contrasting with its dimeric form in solution.
Conclusions:
- The structural similarity and key differences provide insights into glycosylasparaginase function and substrate binding.
- The bacterial enzyme's structure aids in evaluating disease-causing mutations in the human enzyme.
- Flavobacterium meningosepticum glycosylasparaginase is a suitable model for functional analysis and drug development research.
More Related Videos
08:37The Application of Open Searching-based Approaches for the Identification of Acinetobacter baumannii O-linked Glycopeptides
Published on: November 2, 2021
13:35Structural Biology and Analytical Chemistry Approaches for Characterizing C-Glycoside Metabolic Enzymes in Human Gut Microbiota
Published on: May 23, 2025
Related Concept Videos
Protein Glycosylation
Glycosylation occurs in...
Oligosaccharide Assembly
Multiple sugar molecules that may or may...
Proteoglycans
Glycosaminoglycans
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
Peptidoglycan Synthesis
Archaeal Cell Wall