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Molecular recognition of the beta-glucans laminarin and pustulan by a SusD-like glycan-binding protein of a marine Bacteroidetes.

FEBS J.. 2018-10; 
MystkowskaAgata Anna,RobbCraig,Vidal-MelgosaSilvia,VanniChiara,Fernandez-GuerraAntonio,HöhneMatthias,HehemannJan-Hen
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Gene Synthesis … The recombinant plasmid pET28 (a+) containing GMSusD (NCBI Reference Sequence: WP_089661789, residues from 41-501) from Gramella sp. MAR 2010 102 and SusD-like protein from Salegentibacter were obtained by gene synthesis (GenScript) … Get A Quote

摘要

Marine bacteria catabolize carbohydrate polymers of algae, which synthesize these structurally diverse molecules in ocean surface waters. Although algal glycans are an abundant carbon and energy source in the ocean, the molecular details that enable specific recognition between algal glycans and bacterial degraders remain largely unknown. Here we characterized a surface protein, GMSusD from the planktonic Bacteroidetes-Gramella sp. MAR_2010_102 that thrives during algal blooms. Our biochemical and structural analyses show that GMSusD binds glucose polysaccharides such as branched laminarin and linear pustulan. The 1.8 Å crystal structure of GMSusD indicates that three tryptophan residues form the putativ... More

关键词

Bacteroidetes ,carbohydrate-binding proteins,laminarin,microalgae,polysacchar