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- W2897068897 abstract "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, GMS usD from the planktonic Bacteroidetes‐Gramella sp. MAR _2010_102 that thrives during algal blooms. Our biochemical and structural analyses show that GMS usD binds glucose polysaccharides such as branched laminarin and linear pustulan. The 1.8 Å crystal structure of GMS usD indicates that three tryptophan residues form the putative glycan‐binding site. Mutagenesis studies confirmed that these residues are crucial for laminarin recognition. We queried metagenomes of global surface water datasets for the occurrence of SusD‐like proteins and found sequences with the three structurally conserved residues in different locations in the ocean. The molecular selectivity of GMS usD underscores that specific interactions are required for laminarin recognition. In conclusion, our findings provide insight into the molecular details of β‐glucan binding by GMS usD and our bioinformatic analysis reveals that this molecular interaction may contribute to glucan cycling in the surface ocean." @default.
- W2897068897 created "2018-10-26" @default.
- W2897068897 creator A5004420169 @default.
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- W2897068897 date "2018-10-28" @default.
- W2897068897 modified "2023-10-17" @default.
- W2897068897 title "Molecular recognition of the beta‐glucans laminarin and pustulan by a SusD‐like glycan‐binding protein of a marine <i>Bacteroidetes</i>" @default.
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- W2897068897 doi "https://doi.org/10.1111/febs.14674" @default.
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