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  • Title: Rhamnogalacturonan lyase reveals a unique three-domain modular structure for polysaccharide lyase family 4.
    Author: McDonough MA, Kadirvelraj R, Harris P, Poulsen JC, Larsen S.
    Journal: FEBS Lett; 2004 May 07; 565(1-3):188-94. PubMed ID: 15135077.
    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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