| Title : Expression, purification, crystallization and preliminary X-ray analysis of tannase from Lactobacillus plantarum. - Wu_2013_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_69_456 |
| Author(s) : Wu M , Peng X , Wen H , Wang Q , Chen Q , McKinstry WJ , Ren B |
| Ref : Acta Crystallographica Sect F Struct Biol Cryst Commun , 69 :456 , 2013 |
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Abstract :
Tannase catalyses the hydrolysis of the galloyl ester bond of tannins to release gallic acid. It belongs to the serine esterases and has wide applications in the food, feed, beverage, pharmaceutical and chemical industries. The tannase from Lactobacillus plantarum was cloned, expressed and purified. The protein was crystallized by the sitting-drop vapour-diffusion method with microseeding. The crystals belonged to space group P1, with unit-cell paramters a = 46.5, b = 62.8, c = 83.8 A, alpha = 70.4, beta = 86.0, gamma = 79.4degre. Although the enzyme exists mainly as a monomer in solution, it forms a dimer in the asymmetric unit of the crystal. The crystals diffracted to beyond 1.60A resolution using synchrotron radiation and a complete data set was collected to 1.65A resolution. |
| PubMedSearch : Wu_2013_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_69_456 |
| PubMedID: 23545659 |
| Gene_locus related to this paper: lacpl-tanL |
| Inhibitor | 3,4-dihydroxybenzoate Gallate |
| Substrate | Ethyl-Gallate |
| Gene_locus | lacpl-tanL |
| Structure | 4J0J 4J0K 4J0C 4J0D 4J0G 4J0H 4J0I 4JUI |
Wu M, Peng X, Wen H, Wang Q, Chen Q, McKinstry WJ, Ren B (2013)
Expression, purification, crystallization and preliminary X-ray analysis of tannase from Lactobacillus plantarum.
Acta Crystallographica Sect F Struct Biol Cryst Commun
69 :456
Wu M, Peng X, Wen H, Wang Q, Chen Q, McKinstry WJ, Ren B (2013)
Acta Crystallographica Sect F Struct Biol Cryst Commun
69 :456