GH1-family 6-P-β-glucosidases from human microbiome lactic acid bacteria

Michalska, Karolina; Tan, Kemin; Li, Hui; Hatzos-Skintges, Catherine; Bearden, Jessica; Babnigg, Gyorgy; Joachimiak, Andrzej

doi:10.1107/s0907444912049608

Title: GH1-family 6-P-β-glucosidases from human microbiome lactic acid bacteria

Journal Article · Sat Feb 16 00:00:00 EST 2013 · Acta Crystallographica. Section D: Biological Crystallography

DOI:https://doi.org/10.1107/s0907444912049608· OSTI ID:1625678

Michalska, Karolina ^[1]; Tan, Kemin ^[1]; Li, Hui ^[1]; Hatzos-Skintges, Catherine ^[1]; Bearden, Jessica ^[1]; Babnigg, Gyorgy ^[1]; Joachimiak, Andrzej ^[1]

Argonne National Lab. (ANL), Argonne, IL (United States)

In lactic acid bacteria and other bacteria, carbohydrate uptake is mostly governed by phosphoenolpyruvate-dependent phosphotransferase systems (PTSs). PTS-dependent translocation through the cell membrane is coupled with phosphorylation of the incoming sugar. After translocation through the bacterial membrane, the β-glycosidic bond in 6'-P-β-glucoside is cleaved, releasing 6-P-β-glucose and the respective aglycon. This reaction is catalyzed by 6-P-β-glucosidases, which belong to two glycoside hydrolase (GH) families: GH1 and GH4. Here, the high-resolution crystal structures of GH1 6-P-β-glucosidases from Lactobacillus plantarum (LpPbg1) and Streptococcus mutans (SmBgl) and their complexes with ligands are reported. Both enzymes show hydrolytic activity towards 60 -P--glucosides. The LpPbg1 structure has been determined in an apo form as well as in a complex with phosphate and a glucose molecule corresponding to the aglycon molecule. The S. mutans homolog contains a sulfate ion in the phosphate-dedicated subcavity. SmBgl was also crystallized in the presence of the reaction product 6-P-β-glucose. For a mutated variant of the S. mutans enzyme (E375Q), the structure of a 6'-P-salicin complex has also been determined. The presence of natural ligands enabled the definition of the structural elements that are responsible for substrate recognition during catalysis.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division

Grant/Contract Number:: AC02-06CH11357

OSTI ID:: 1625678

Journal Information:: Acta Crystallographica. Section D: Biological Crystallography, Vol. 69, Issue 3; ISSN 0907-4449

Publisher:: International Union of CrystallographyCopyright Statement

Country of Publication:: United States

Language:: English

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