3WA7: Crystal Structure Of Selenomethionine-labeled Tannase From Lactobacillus Plantarum In The Orthorhombic Crystal

Citation:
Abstract
Tannin acylhydrolase (EC 3.1.1.20) referred commonly as tannase catalyzes the hydrolysis of the galloyl ester bond of tannins to release gallic acid. Although the enzyme is useful for various industries, the tertiary structure is not yet determined. In this study, we determined the crystal structure of tannase produced by Lactobacillus plantarum. The tannase structure belongs to a member of alpha/beta-hydrolase superfamily with an additional "lid" domain. A glycerol molecule derived from cryoprotectant solution was accommodated into the tannase active site. The binding manner of glycerol to tannase seems to be similar to that of the galloyl moiety in the substrate. Proteins 2013; 81:2052-2058. (c) 2013 Wiley Periodicals, Inc.
PDB ID: 3WA7Download
MMDB ID: 111961
PDB Deposition Date: 2013/4/27
Updated in MMDB: 2013/11
Experimental Method:
x-ray diffraction
Resolution: 1.7  Å
Source Organism:
Similar Structures:
Biological Unit for 3WA7: monomeric; determined by author and by software (PISA)
Molecular Components in 3WA7
Label Count Molecule
Protein (1 molecule)
1
Tannase
Molecule annotation
Chemicals (5 molecules)
1
2
2
1
3
2
* Click molecule labels to explore molecular sequence information.

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