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How a Glycoside Hydrolase Recognizes a Helical Polyglucan
Bernard Henrissat1, Marie-Line Garron2
1Architecture et Fonction des Macromolécules Biologiques, CNRS, Aix-Marseille Université, 13288 Marseille, France; INRA, USC 1408 AFMB, F-13288 Marseille, France; Department of Biological Sciences, King Abdulaziz University, Jeddah, Saudi Arabia.
Structure (London, England : 1993)
|September 7, 2017
Summary
Enzymes called glycoside hydrolases (GH) can recognize the complex helical structures of polysaccharides. This study reveals the structural basis for how GH81 enzymes interact with these polysaccharide quaternary structures.
Area of Science:
- Biochemistry
- Structural Biology
- Carbohydrate Chemistry
Background:
- Linear polysaccharides can adopt complex double- or triple-helical quaternary structures.
- The enzymatic recognition and processing of these complex polysaccharide structures remain poorly understood.
Purpose of the Study:
- To investigate the structural basis for enzyme-substrate interactions involving polysaccharide quaternary structures.
- To elucidate how glycoside hydrolase family 81 (GH81) enzymes recognize and bind to helical polysaccharides.
Main Methods:
- Structural analysis of GH81 enzymes.
- Biochemical assays to assess enzyme activity on polysaccharide substrates.
- Molecular modeling to understand enzyme-substrate complementarity.
Main Results:
- Pluvinage et al. (2017) identified specific structural features enabling GH81 enzymes to bind helical polysaccharides.
- The study highlights the importance of structural complementarity between the enzyme's active site and the polysaccharide's quaternary structure.
- Evidence suggests a mechanism for selective recognition of specific polysaccharide conformations.
Conclusions:
- GH81 enzymes possess unique structural adaptations for interacting with polysaccharide quaternary structures.
- Understanding this interaction provides insights into enzymatic degradation and modification of complex carbohydrates.
- This work advances our knowledge of enzyme specificity in carbohydrate processing.
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