9ku5 | pdb_00009ku5

Crystal structure of substrate bound GH5_22 exo-beta-xylosidase from the seaweed-derived thermophile Geobacillus thermodenitrificans OS27

spinqualitylabelsall models 9ku5, resolution 1.52Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9ku5 is a 2 chain structure with sequence from Geobacillus thermodenitrificans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.52Å Ligands: FE, GOL, PRD_900117, XYP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Geobacillus thermodenitrificans OS27 is a seaweed-derived thermophile that harbors a GH5_22 gene (bxlA) that encodes for a glycoside hydrolase fused with the cyclin box domain. In this study, we characterized the catalytic activity, enzymatic properties, three-dimensional structure, and physiological role of the gene product, GtBxlA. The enzyme was produced as a thermostable dimer, acting on p-nitrophenyl-beta-d-xylopyranoside among 23 substrates. beta-1,4-Linked xylooligosaccharides were also hydrolyzed from the nonreducing end. The activity indicated that GtBxlA functions as an exo-beta-1,4-xylosidase. We determined the crystal structure of the Glu188Ala variant complexed with beta-1,4-xylotriose at 1.52 A resolution. GtBxlA exhibited an atypical (beta/alpha)(8)-barrel architecture. The cyclin box constituted a single alpha-helix within the core barrel and a lid-like domain that contributes to dimer formation. Structural analysis revealed that Glu188 and Glu318 are positioned to serve as the acid/base and nucleophile catalysts, respectively. Alanine mutagenesis confirmed the essential role of Glu188 and Glu318 in catalysis. We also determined the ligand-free structure of the Glu188Ala variant. Both structures were almost identical; however, a loop at the substrate entry site was fixed in the ligand-free structure, suggesting a conformational change upon substrate binding. Although bxlA deletion did not affect beta-1,4-xylan utilization, its expression was induced by beta-1,4-xylan. These observations suggest that G. thermodenitrificans OS27 employed GtBxlA in utilizing beta-1,4-xylan. Notably, GtBxlA could hydrolyze beta-1,3-linked xylooligosaccharides. This highlights the possibility that GtBxlA also assists the host in utilizing beta-1,3-xylan, which is abundant in certain seaweeds. Structural and biochemical characterization of a GH5_22 enzyme from the seaweed-derived thermophile Geobacillus thermodenitrificans OS27.,Lee W, Hino T, Fujii K, Tanimoto S, Naka R, Hara K, Okamoto T, Okazaki F, Nagano S, Ohshiro T, Suzuki H Arch Biochem Biophys. 2026 Jan 16;778:110736. doi: 10.1016/j.abb.2026.110736. PMID:41548701 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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