5jbf

4,6-alpha-glucanotransferase GTFB (D1015N mutant) from Lactobacillus reuteri 121 complexed with maltopentaose

spinqualitylabelsall models 5jbf, resolution 2.19Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5jbf is a 2 chain structure with sequence from Limosilactobacillus reuteri. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.19Å Ligands: CA, GLC, PRD_900001, PRD_900009, PRD_900030, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5SBM0_LIMRT Publication Abstract from PubMed Food processing and refining has dramatically changed the human diet, but little is known about whether this affected the evolution of enzymes in human microbiota. We present evidence that glycoside hydrolase family 70 (GH70) glucansucrases from lactobacilli, synthesizing alpha-glucan-type extracellular polysaccharides from sucrose, likely evolved from GH13 starch-acting alpha-amylases, via GH70 4,6-alpha-glucanotransferases. The crystal structure of a 4,6-alpha-glucanotransferase explains the mode of action and unique product specificity of these enzymes. While the alpha-amylase substrate-binding scaffold is retained, active-site loops adapted to favor transglycosylation over hydrolysis; the structure also gives clues as to how 4,6-alpha-glucanotransferases may have evolved further toward sucrose utilization instead of starch. Further supported by genomic, phylogenetic, and in vivo studies, we propose that dietary changes involving starch (and starch derivatives) and sucrose intake were critical factors during the evolution of 4,6-alpha-GTs and glucansucrases from alpha-amylases, allowing oral bacteria to produce extracellular polymers that contribute to biofilm formation from different substrates. Crystal Structure of 4,6-alpha-Glucanotransferase Supports Diet-Driven Evolution of GH70 Enzymes from alpha-Amylases in Oral Bacteria.,Bai Y, Gangoiti J, Dijkstra BW, Dijkhuizen L, Pijning T Structure. 2016 Dec 21. pii: S0969-2126(16)30390-2. doi:, 10.1016/j.str.2016.11.023. PMID:28065507 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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