ArticleNature structural & molecular biology2024
The Ruminococcus bromii amylosome protein Sas6 binds single and double helical α-glucan structures in starch.
Article in Nature structural & molecular biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Mechanistic insights into substrate-targeting modification effects on interfacial kinetics of raw starch-degrading amylases.Applied and environmental microbiology · 2026Article
- Gatekeeping Dietary Fiber: The Role of Carbohydrate-Binding Modules in the Human Gut.Journal of microbiology and biotechnology · 2026Review
- Bifidobacterial genes upregulated by resistant starch investigated using multi-omics have orthologs in infant gut isolates.ISME communications · 2026Article
- Spatial constraints drive amylosome-mediated resistant starch degradation by Ruminococcus bromii in the human colon.Nature communications · 2025Article
- Bacterial interactions on nutrient-rich surfaces in the gut lumen.Infection and immunity · 2024Review
- Nutrient acquisition strategies by gut microbes.Cell host & microbe · 2024Review
- Article
- Presence of digestible starch impactsFood & function · 2024Article
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Authors and funding
12 authors at 5 institutions in 2 countries.
Funding
Abstract
Resistant starch is a prebiotic accessed by gut bacteria with specialized amylases and starch-binding proteins. The human gut symbiont Ruminococcus bromii expresses Sas6 (Starch Adherence System member 6), which consists of two starch-specific carbohydrate-binding modules from family 26 (RbCBM26) and family 74 (RbCBM74). Here, we present the crystal structures of Sas6 and of RbCBM74 bound with a double helical dimer of maltodecaose. The RbCBM74 starch-binding groove complements the double helical α-glucan geometry of amylopectin, suggesting that this module selects this feature in starch granules. Isothermal titration calorimetry and native mass spectrometry demonstrate that RbCBM74 recognizes longer single and double helical α-glucans, while RbCBM26 binds short maltooligosaccharides. Bioinformatic analysis supports the conservation of the amylopectin-targeting platform in CBM74s from resistant-starch degrading bacteria. Our results suggest that RbCBM74 and RbCBM26 within Sas6 recognize discrete aspects of the starch granule, providing molecular insight into how this structure is accommodated by gut bacteria.
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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.