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

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Mystkowska,  Agata Anna
University Bremen - MPI Joint Research Group for Marine Glycobiology, Max Planck Institute for Marine Microbiology, Max Planck Society;

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Robb,  Craig
University Bremen - MPI Joint Research Group for Marine Glycobiology, Max Planck Institute for Marine Microbiology, Max Planck Society;

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Vidal-Melgosa,  Silvia
University Bremen - MPI Joint Research Group for Marine Glycobiology, Max Planck Institute for Marine Microbiology, Max Planck Society;

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Vanni,  Chiara
Microbial Genomics Group, Department of Molecular Ecology, Max Planck Institute for Marine Microbiology, Max Planck Society;

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Fernandez-Guerra,  Antonio
Microbial Genomics Group, Department of Molecular Ecology, Max Planck Institute for Marine Microbiology, Max Planck Society;

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Hehemann,  Jan Hendrik
University Bremen - MPI Joint Research Group for Marine Glycobiology, Max Planck Institute for Marine Microbiology, Max Planck Society;

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Citation

Mystkowska, A. A., Robb, C., Vidal-Melgosa, S., Vanni, C., Fernandez-Guerra, A., Höhne, M., et al. (2018). Molecular recognition of the beta-glucans laminarin and pustulan by a SusD-like glycan-binding protein of a marine Bacteroidetes. The FEBS Journal, 285(23), 4465-4481. doi:10.1111/febs.14674.


Cite as: http://hdl.handle.net/21.11116/0000-0003-B84C-9
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, 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 angstrom crystal structure of GMSusD 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 GMSusD underscores that specific interactions are required for laminarin recognition. In conclusion, our findings provide insight into the molecular details of beta-glucan binding by GMSusD and our bioinformatic analysis reveals that this molecular interaction may contribute to glucan cycling in the surface ocean.