ArticleThe Journal of biological chemistry2022
Sas20 is a highly flexible starch-binding protein in the Ruminococcus bromii cell-surface amylosome.
Article in The Journal of biological chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- Gut microbial dynamics and antibiotic resistance during rifaximin therapy in severe cirrhosis: a ProPILA-Rifax ancillary study.Frontiers in cellular and infection microbiology · 2026Trial
- Gatekeeping Dietary Fiber: The Role of Carbohydrate-Binding Modules in the Human Gut.Journal of microbiology and biotechnology · 2026Review
- Spatial constraints drive amylosome-mediated resistant starch degradation by Ruminococcus bromii in the human colon.Nature communications · 2025Article
- The effects of Astragalus, Epimedium, and Fructus Ligustri Lucidi extract on the antioxidant capacity, and immune status of goslings under stress conditions.Frontiers in veterinary science · 2025Article
- Bacterial interactions on nutrient-rich surfaces in the gut lumen.Infection and immunity · 2024Review
- Understanding the gut microbiota by considering human evolution: a story of fire, cereals, cooking, molecular ingenuity, and functional cooperation.Microbiology and molecular biology reviews : MMBR · 2024Review
- Article
- The Ruminococcus bromii amylosome protein Sas6 binds single and double helical α-glucan structures in starch.Nature structural & molecular biology · 2024Article
- Article
- Isothermal Titration Calorimetry for Quantification of Protein-Carbohydrate Interactions.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Sticking to starch.The Journal of biological chemistry · 2022Article
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Authors and funding
12 authors at 5 institutions in 2 countries.
Funding
Abstract
Ruminococcus bromii is a keystone species in the human gut that has the rare ability to degrade dietary resistant starch (RS). This bacterium secretes a suite of starch-active proteins that work together within larger complexes called amylosomes that allow R. bromii to bind and degrade RS. Starch adherence system protein 20 (Sas20) is one of the more abundant proteins assembled within amylosomes, but little could be predicted about its molecular features based on amino acid sequence. Here, we performed a structure-function analysis of Sas20 and determined that it features two discrete starch-binding domains separated by a flexible linker. We show that Sas20 domain 1 contains an N-terminal β-sandwich followed by a cluster of α-helices, and the nonreducing end of maltooligosaccharides can be captured between these structural features. Furthermore, the crystal structure of a close homolog of Sas20 domain 2 revealed a unique bilobed starch-binding groove that targets the helical α1,4-linked glycan chains found in amorphous regions of amylopectin and crystalline regions of amylose. Affinity PAGE and isothermal titration calorimetry demonstrated that both domains bind maltoheptaose and soluble starch with relatively high affinity (K
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.