Wu_2013_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_69_456

Reference

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
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

Related information

Inhibitor 3,4-dihydroxybenzoate    Gallate
Substrate Ethyl-Gallate
Gene_locus lacpl-tanL
Structure 4J0J    4J0K    4J0C    4J0D    4J0G    4J0H    4J0I    4JUI

Citations formats

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