
pmid: 15135077
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.
Models, Molecular, Protein Conformation, Molecular Sequence Data, Family 4 polysaccharide lyase, Crystallography, X-Ray, Rhamnose, Catalysis, Protein Structure, Secondary, Substrate Specificity, Carbohydrate active enzyme, Cell Wall, Catalytic Domain, Amino Acid Sequence, Polysaccharide-Lyases, Sequence Homology, Amino Acid, Hexuronic Acids, Pectin degradation, Rhamnogalacturonan, X-ray crystal structure, Protein Structure, Tertiary, Aspergillus, Pectins, Peptides, Plant cell wall polysaccharide, Protein Binding
Models, Molecular, Protein Conformation, Molecular Sequence Data, Family 4 polysaccharide lyase, Crystallography, X-Ray, Rhamnose, Catalysis, Protein Structure, Secondary, Substrate Specificity, Carbohydrate active enzyme, Cell Wall, Catalytic Domain, Amino Acid Sequence, Polysaccharide-Lyases, Sequence Homology, Amino Acid, Hexuronic Acids, Pectin degradation, Rhamnogalacturonan, X-ray crystal structure, Protein Structure, Tertiary, Aspergillus, Pectins, Peptides, Plant cell wall polysaccharide, Protein Binding
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