Crystallization (Comment) | Organism |
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crystals of mutant D229 soaked with aryl glycoside substrate 4-nitrophenyl alpha-L-fucoside. X-ray data at 1.95 A resolution reveal an unambiguous electron density for the unhydrolysed substrate, which is in the 1C4 conformation. Trapping of fucosyl-enzyme intermediate on the E288Q variant and analysis at 2.1 A. Again, the observed electron density reveals the trapped beta-L-fucosyl enzyme intermediate, here in the 3S1 conformation with the beta-linkage to the nucleophile Asp229 | Bacteroides thetaiotaomicron |
Protein Variants | Comment | Organism |
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D229N | inactive, mutation of the catalytic nucleophile. Crystallization data | Bacteroides thetaiotaomicron |
E288Q | acid/base variant, crystallization data in complex with substrate 2-fluoro fucosyl fluoride | Bacteroides thetaiotaomicron |
Organism | UniProt | Comment | Textmining |
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Bacteroides thetaiotaomicron | - |
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Bacteroides thetaiotaomicron Bt2970 | - |
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Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
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additional information | series of snapshots of the reaction coordinate. The Michaelis complex is observed in a 1C4 conformation, and a trapped covalent intermediate in the 3S1 skew boat which together provides structural evidence for a latitudinal Southern Hemisphere 1C4-3H4-3S1 pathway for terminal alpha-L-fucoside hydrolysis | Bacteroides thetaiotaomicron | ? | - |
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additional information | series of snapshots of the reaction coordinate. The Michaelis complex is observed in a 1C4 conformation, and a trapped covalent intermediate in the 3S1 skew boat which together provides structural evidence for a latitudinal Southern Hemisphere 1C4-3H4-3S1 pathway for terminal alpha-L-fucoside hydrolysis | Bacteroides thetaiotaomicron Bt2970 | ? | - |
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