Journal
STRUCTURE
Volume 16, Issue 7, Pages 1105-1115Publisher
CELL PRESS
DOI: 10.1016/j.str.2008.03.017
Keywords
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Funding
- NIDDK NIH HHS [R37 DK030292, DK30292, R01 DK030292] Funding Source: Medline
- NIGMS NIH HHS [F32 GM078800, GM078800, F32 GM078800-02] Funding Source: Medline
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The human gut microbiota performs functions that are not encoded in our Homo sapiens genome, including the processing of otherwise undigestible dietary polysaccharides. Defining the structures of proteins involved in the import and degradation of specific glycans by saccharolytic bacteria complements genomic analysis of the nutrient-processing capabilities of gut communities. Here, we describe the atomic structure of one such protein, SusD, required for starch binding and utilization by Bacteroides thetaiotaomicron, a prominent adaptive forager of glycans in the distal human gut microbiota. The binding pocket of this unique alpha-helical protein contains an arc of aromatic residues that complements the natural helical structure of starch and imposes this conformation on bound maltoheptaose. Furthermore, SusD binds cyclic oligosaccharides with higher affinity than linear forms. The structures of several SusD/oligosaccharide complexes reveal an inherent ligand recognition plasticity dominated by the three-dimensional conformation of the oligosaccharides rather than specific interactions with the composite sugars.
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