6b3p

Crystal structure of CBMbc (family CBM26) from Eubacterium rectale Amy13K in Complex with Maltoheptaose

spinqualitylabelsall models 6b3p, resolution 2.01Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6b3p is a 2 chain structure with sequence from Eubacterium rectale M104/1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.01Å Ligands: EDO, FMT, GLC, PRD_900009, PRD_900010 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D4JJZ5_9FIRM Publication Abstract from PubMed Gut bacteria recognize accessible glycan substrates within a complex environment. Carbohydrate binding modules (CBMs) of cell-surface glycoside hydrolases often drive binding to the target substrate. Eubacterium rectale, an important butyrate-producing organism in the gut, consumes a limited range of substrates, including starch. Host consumption of resistant starch increases the abundance of E. rectale in the intestine, likely because it successfully captures the products of resistant starch degradation by other bacteria. Here we demonstrate that the cell wall anchored starch-degrading alpha-amylase, Amy13K of E. rectale harbors five CBMs that all target starch with differing specificities. Intriguingly these CBMs efficiently bind to both regular and high amylose corn starch (a type of resistant starch), but have almost no affinity for potato starch (another type of resistant starch). Removal of these CBMs from Amy13K reduces the activity level of the enzyme towards corn starches by approximately 40-fold, down to the level of activity towards potato starch, suggesting that the CBMs facilitate activity on corn starch and allowing its utilization in vivo. The specificity of the Amy13K CBMs provides a molecular rationale for why E. rectale is able to only use certain starch types without the aid of other organisms. Novel carbohydrate binding modules in the surface anchored alpha-amylase of Eubacterium rectale provide a molecular rationale for the range of starches used by this organism in the human gut.,Cockburn DW, Suh C, Medina KP, Duvall RM, Wawrzak Z, Henrissat B, Koropatkin NM Mol Microbiol. 2017 Nov 15. doi: 10.1111/mmi.13881. PMID:29139580 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cyclin-dependent kinase 3D structures

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