Sas20 is a highly flexible starch-binding protein in the Ruminococcus bromii cell-surface amylosome
Filipe M. Cerqueira, Amanda Photenhauer, Heidi L. Doden, Aric N. Brown, Ahmed M. Abdel-Hamid, Sarah Moraïs, Edward A. Bayer, Z. Wawrzak, Isaac Cann, Jason M. Ridlon, Jesse B. Hopkins, Nicole M. Koropatkin
Abstract
≤ 20 μM) but exhibit limited or no binding to cyclodextrins. Finally, small-angle X-ray scattering analysis of the individual and combined domains support that these structures are highly flexible, which may allow the protein to adopt conformations that enhance its starch-targeting efficiency. Taken together, we conclude that Sas20 binds distinct features within the starch granule, facilitating the ability of R. bromii to hydrolyze dietary RS.
Topics & Concepts
Isothermal titration calorimetryAmyloseStarchAmylopectinLinkerBiochemistryCrystallographyChemistryBiophysicsStereochemistryBiologyComputer scienceOperating systemFood composition and propertiesEnzyme Production and CharacterizationMicrobial Metabolites in Food Biotechnology