Rhamnogalacturonan lyase reveals a unique three-domain modular structure for polysaccharide lyase family 4

Michael A. McDonough, Renuka Kadirvelraj, Pernille Harris, Jens-Christian N. Poulsen, Sine Larsen

Research output: Contribution to journalJournal articleResearchpeer-review

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 rhamno galacturonan-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 Angstrom 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.
Original languageEnglish
JournalFEBS Letters
Volume565
Pages (from-to)188-194
ISSN0014-5793
Publication statusPublished - 2004

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