![]() ![]() high-performance anion exchange chromatography with pulsed amperometric detection.In conclusion, our findings provide insight into the molecular details of β-glucan binding by GMSusD and our bioinformatic analysis reveals that this molecular interaction may contribute to glucan cycling in the surface ocean. The molecular selectivity of GMSusD underscores that specific interactions are required 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. Mutagenesis studies confirmed that these residues are crucial for laminarin recognition. The 1.8 Å crystal structure of GMSusD indicates that three tryptophan residues form the putative glycan-binding site. Our biochemical and structural analyses show that GMSusD binds glucose polysaccharides such as branched laminarin and linear pustulan. MAR_2010_102 that thrives during algal blooms. Here we characterized a surface protein, GMSusD from the planktonic Bacteroidetes-Gramella sp. 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. Marine bacteria catabolize carbohydrate polymers of algae, which synthesize these structurally diverse molecules in ocean surface waters. ![]()
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