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• W2015600669 abstract "The beta-galactosidase from an extreme thermophile, Thermus thermophilus A4 (A4-beta-Gal), is thermostable and belongs to the glycoside hydrolase family 42 (GH-42). As the first known structures of a GH-42 enzyme, we determined the crystal structures of free and galactose-bound A4-beta-Gal at 1.6A and 2.2A resolution, respectively. A4-beta-Gal forms a homotrimeric structure resembling a flowerpot. Each monomer has an active site located inside a large central tunnel. The N-terminal domain of A4-beta-Gal has a TIM barrel fold, as predicted from hydrophobic cluster analysis. The putative catalytic residues of A4-beta-Gal (Glu141 and Glu312) superimpose well with the catalytic residues of Escherichia coli beta-galactosidase. The environment around the catalytic nucleophile (Glu312) is similar to that in the case of E.coli beta-galactosidase, but the recognition mechanism for a substrate is different. Trp182 of the next subunit of the trimer constitutes a part of the active-site pocket, indicating that the trimeric structure is essential for the enzyme activity. Structural comparison with other glycoside hydrolases revealed that many features of the 4/7 superfamily are conserved in the A4-beta-Gal structure. On the basis of the results of 1H NMR spectroscopy, A4-beta-Gal was determined to be a retaining enzyme. Interestingly, the active site was similar with those of retaining enzymes, but the overall fold of the TIM barrel domain was very similar to that of an inverting enzyme, beta-amylase." @default.
• W2015600669 created "2016-06-24" @default.
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• W2015600669 date "2002-09-01" @default.
• W2015600669 modified "2023-10-13" @default.
• W2015600669 title "Trimeric Crystal Structure of the Glycoside Hydrolase Family 42 β-Galactosidase from Thermus thermophilus A4 and the Structure of its Complex with Galactose" @default.
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• W2015600669 doi "https://doi.org/10.1016/s0022-2836(02)00746-5" @default.
• W2015600669 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12215416" @default.
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