AI Article Synopsis
- Plant β-galactosidases, like tomato β-galactosidase 4 (TBG4), are crucial for various processes such as mobilizing carbohydrate reserves and aiding in cell-wall expansion during ripening.
- TBG4 is unique because it has both β-galactosidase and exo-β-(1,4)-galactanase activities, specifically targeting longer β-(1,4)-galactans, unlike most similar enzymes that focus only on the former activity.
- The TBG4 protein was successfully crystallized using a specific method, resulting in orthorhombic crystals that diffracted at a high resolution of 1.65 Å,
Article Abstract
Plant β-galactosidases play important roles in carbohydrate-reserve mobilization, cell-wall expansion and degradation, and turnover of signalling molecules during ripening. Tomato β-galactosidase 4 (TBG4) not only has β-galactosidase activity but also has exo-β-(1,4)-galactanase activity, and prefers β-(1,4)-galactans longer than pentamers as its substrates; most other β-galactosidases only have the former activity. Recombinant TBG4 protein expressed in the yeast Pichia pastoris was crystallized by the sitting-drop vapour-diffusion method using PEG 10,000 as a precipitant. The crystals belonged to the orthorhombic space group P212121, with unit-parameters a = 92.82, b = 96.30, c = 159.26 Å, and diffracted to 1.65 Å resolution. Calculation of the Matthews coefficient suggested the presence of two monomers per asymmetric unit (VM = 2.2 Å(3) Da(-1)), with a solvent content of 45%.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4321468 | PMC |
| http://dx.doi.org/10.1107/S2053230X14027800 | DOI Listing |
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