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FEBS Letters
Article . 2004 . Peer-reviewed
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FEBS Letters
Article . 2004
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Rhamnogalacturonan lyase reveals a unique three‐domain modular structure for polysaccharide lyase family 4

Authors: Pernille Harris; Michael A. McDonough; Jens-Christian N. Poulsen; Sine Larsen; Sine Larsen; Renuka Kadirvelraj;

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

Abstract

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.

Keywords

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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    This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
    Top 10%
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citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
49
Top 10%
Top 10%
Top 10%
bronze