9bal

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Surface glycan-binding protein A (SGBP-A, SusD-like) from a mixed-linkage beta-glucan utilization locus in Segatella copri in complex with cellopentaoseSurface glycan-binding protein A (SGBP-A, SusD-like) from a mixed-linkage beta-glucan utilization locus in Segatella copri in complex with cellopentaose

Structural highlights

9bal is a 1 chain structure with sequence from Segatella copri DSM 18205. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.5Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

D1PD12_9BACT

Publication Abstract from PubMed

Mixed-linkage beta(1,3)/beta(1,4)-glucan (MLG) is abundant in the human diet through the ingestion of cereal grains and is widely associated with healthful effects on metabolism and cholesterol levels. MLG is also a major source of fermentable glucose for the human gut microbiota (HGM). Bacteria from the family Prevotellaceae are highly represented in the HGM of individuals who eat plant-rich diets, including certain indigenous people and vegetarians in postindustrial societies. Here, we have defined and functionally characterized an exemplar Prevotellaceae MLG polysaccharide utilization locus (MLG-PUL) in the type-strain Segatella copri (syn. Prevotella copri) DSM 18205 through transcriptomic, biochemical, and structural biological approaches. In particular, structure-function analysis of the cell-surface glycan-binding proteins and glycoside hydrolases of the S. copri MLG-PUL revealed the molecular basis for glycan capture and saccharification. Notably, syntenic MLG-PULs from human gut, human oral, and ruminant gut Prevotellaceae are distinguished from their counterparts in Bacteroidaceae by the presence of a beta(1,3)-specific endo-glucanase from glycoside hydrolase family 5, subfamily 4 (GH5_4) that initiates MLG backbone cleavage. The definition of a family of homologous MLG-PULs in individual species enabled a survey of nearly 2000 human fecal microbiomes using these genes as molecular markers, which revealed global population-specific distributions of Bacteroidaceae- and Prevotellaceae-mediated MLG utilization. Altogether, the data presented here provide new insight into the molecular basis of beta-glucan metabolism in the HGM, as a basis for informing the development of approaches to improve the nutrition and health of humans and other animals.

The molecular basis of cereal mixed-linkage beta-glucan utilization by the human gut bacterium Segatella copri.,Golisch B, Cordeiro RL, Fraser ASC, Briggs J, Stewart WA, Van Petegem F, Brumer H J Biol Chem. 2024 Sep;300(9):107625. doi: 10.1016/j.jbc.2024.107625. Epub 2024 , Aug 8. PMID:39122003[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Golisch B, Cordeiro RL, Fraser ASC, Briggs J, Stewart WA, Van Petegem F, Brumer H. The molecular basis of cereal mixed-linkage β-glucan utilization by the human gut bacterium Segatella copri. J Biol Chem. 2024 Sep;300(9):107625. PMID:39122003 doi:10.1016/j.jbc.2024.107625

9bal, resolution 1.50Å

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OCA