Download MendeleyRhamnogalacturonan lyase reveals a unique three-domain modular structure for polysaccharide lyase family 4.
McDonough, M.A., Kadirvelraj, R., Harris, P., Poulsen, J.C., Larsen, S.(2004) FEBS Lett 565: 188-194
- PubMed: 15135077
- DOI: https://doi.org/10.1016/j.febslet.2004.03.094
- Primary Citation of Related Structures:
1NKG - PubMed 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.
Organizational Affiliation:
Centre for Crystallographic Studies, University of Copenhagen, Universitetsparken 5, 2100 Copenhagen Ø, DK, Denmark. michael.mcdonough@chemistry.oxford.ac.uk
