6r5o | pdb_00006r5o

The crystal structure the Glycoside Hydrolase BglX inactive mutant D286N from P. aeruginosa in complex with two glucose molecules

spinqualitylabelsall models 6r5o, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6r5o is a 2 chain structure with sequence from Pseudomonas aeruginosa PAO1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: BGC, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9I311_PSEAE Publication Abstract from PubMed BglX is a heretofore uncharacterized periplasmic glycoside hydrolase (GH) of the human pathogen Pseudomonas aeruginosa. X-ray analysis identifies it as a protein homodimer. The two active sites of the homodimer comprise catalytic residues provided by each monomer. This arrangement is seen in <2% of the hydrolases of known structure. In vitro substrate profiling shows BglX is a catalyst for beta-(1-->2) and beta-(1-->3) saccharide hydrolysis. Saccharides with beta-(1-->4) or beta-(1-->6) bonds, and the beta-(1-->4) muropeptides from the cell-wall peptidoglycan, are not substrates. Additional structural insights from X-ray analysis (including structures of a mutant enzyme-derived Michaelis complex, two transition-state mimetics, and two enzyme-product complexes) enabled the comprehensive description of BglX catalysis. The half-chair ((4)H3) conformation of the transition-state oxocarbenium species, the approach of the hydrolytic water molecule to the oxocarbenium species, and the stepwise release of the two reaction products were also visualized. The substrate pattern for BglX aligns with the [beta-(1-->2)-Glc]x and [beta-(1-->3)-Glc]x periplasmic osmoregulated periplasmic glucans, and possibly with the Psl exopolysaccharides, of P. aeruginosa. Both polysaccharides are implicated in biofilm formation. Accordingly, we show that inactivation of the bglX gene of P. aeruginosa PAO1 attenuates biofilm formation. Catalytic Cycle of Glycoside Hydrolase BglX from Pseudomonas aeruginosa and Its Implications for Biofilm Formation.,Mahasenan KV, Batuecas MT, De Benedetti S, Kim C, Rana N, Lee M, Hesek D, Fisher JF, Sanz-Aparicio J, Hermoso JA, Mobashery S ACS Chem Biol. 2020 Jan 17;15(1):189-196. doi: 10.1021/acschembio.9b00754. Epub, 2020 Jan 7. PMID:31877028 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-glucosidase 3D structures

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