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Rhamnogalacturonan lyase reveals a unique three‐domain modular structure for polysaccharide lyase family 4
Author(s) -
McDonough Michael A.,
Kadirvelraj Renuka,
Harris Pernille,
Poulsen Jens-Christian N.,
Larsen Sine
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.03.094
Subject(s) - lyase , cell wall , biochemistry , glycosidic bond , polysaccharide , enzyme , chemistry , glycoside hydrolase , rhamnose , stereochemistry , pectin lyase , pectinase
Rhamnogalacturonan lyase (RG‐lyase) specifically recognizes and cleaves α‐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 Å 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.