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Structural Characterization of Mannan Cell Wall Polysaccharides in Plants Using PACE
Published on: October 16, 2017
Rhamnogalacturonan lyase reveals a unique three-domain modular structure for polysaccharide lyase family 4
Michael A McDonough1, Renuka Kadirvelraj, Pernille Harris
1Centre for Crystallographic Studies, University of Copenhagen, Universitetsparken 5, 2100 Copenhagen Ø, DK, Denmark. michael.mcdonough@chemistry.oxford.ac.uk
Abstract:
Rhamnogalacturonan lyase (RG-lyase) specifically recognizes and cleaves alpha-1,4 glycosidic bonds between L-rhamnose and D-galacturonic acids in the backbone of rhamnogalacturonan-I, a major component of the plant cell wall polysaccharide, pectin. The three-dimensional structure of RG-lyase from Aspergillus aculeatus has been determined to 1.5 A resolution representing the first known structure from polysaccharide lyase family 4 and of an enzyme with this catalytic specificity. The 508-amino acid polypeptide displays a unique arrangement of three distinct modular domains. Each domain shows structural homology to non-catalytic domains from other carbohydrate active enzymes.
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