7f3a

Arabidopsis thaliana GH1 beta-glucosidase AtBGlu42

spinqualitylabelsall models 7f3a, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7f3a is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BGL42_ARATH Glucosidase that hydrolyzes scopolin and various beta-glucosides, cellooligosaccharides (mainly cellotriose) and laminarioligosaccharides (PubMed:34965581). Can use p-nitrophenyl-beta-glucosides (pNP beta-Glc) and p-nitrophenyl-beta-D-fucosides (pNP beta-D-Fuc) as substrates, and, to a lower extent, beta-galactosides, beta-mannosides and beta-xylosides (PubMed:34965581). Involved in the secretion of root-derived phenolics upon iron ions (Fe) depletion (PubMed:25138267). Promotes disease resistance toward B.cinerea, H.arabidopsidis and P.syringae pv. tomato DC3000 (PubMed:25138267). Required during rhizobacteria-mediated (e.g. P.fluorescens WCS417r) broad-spectrum induced systemic resistance (ISR) against several pathogens (PubMed:25138267). Publication Abstract from PubMed Plants possess many glycoside hydrolase family 1 (GH1) beta-glucosidases, which physiologically function in cell wall metabolism and activation of bioactive substances, but most remain uncharacterized. One GH1 isoenzyme AtBGlu42 in Arabidopsis thaliana has been identified to hydrolyze scopolin using the gene deficient plants, but no enzymatic properties were obtained. Its sequence similarity to another functionally characterized enzyme Os1BGlu4 in rice suggests that AtBGlu42 also acts on oligosaccharides. Here, we show that the recombinant AtBGlu42 possesses high kcat/Km not only on scopolin, but also on various beta-glucosides, cellooligosaccharides, and laminarioligosaccharides. Of the cellooligosaccharides, cellotriose was the most preferred. The crystal structure, determined at 1.7 A resolution, suggests that Arg342 gives unfavorable binding to cellooligosaccharides at subsite +3. The mutants R342Y and R342A showed the highest preference on cellotetraose or cellopentaose with increased affinities at subsite +3, indicating that the residues at this position have an important role for chain length specificity. Substrate specificity of glycoside hydrolase family 1 beta-glucosidase AtBGlu42 from Arabidopsis thaliana and its molecular mechanism.,Horikoshi S, Saburi W, Yu J, Matsuura H, Cairns JRK, Yao M, Mori H Biosci Biotechnol Biochem. 2022 Jan 24;86(2):231-245. doi: 10.1093/bbb/zbab200. PMID:34965581 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-glucosidase 3D structures

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