PDBsum entry 4j0c

Hydrolase

PDB id: 4j0c

Contents

Protein chains

452 a.a.

Ligands

PEG ×5

1PE

Waters ×679

PDB id:

4j0c

Name:

Hydrolase

Title:

Tannin acyl hydrolase from lactobacillus plantarum (native structure)

Structure:

Tannase. Chain: a, b. Engineered: yes

Source:

Lactobacillus plantarum. Organism_taxid: 1590. Gene: tanlpl. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.65Å R-factor: 0.166 R-free: 0.192

Authors:

M.Wu,Q.Wang,X.Peng,H.Wen,Q.Chen,W.J.Mckinstry

Key ref:

B.Ren et al. (2013). Crystal structure of tannase from Lactobacillus plantarum. J Mol Biol, 425, 2737-2751. PubMed id: 23648840 DOI: 10.1016/j.jmb.2013.04.032

Date:

30-Jan-13 Release date: 22-May-13

Protein chains

B3Y018  (B3Y018_LACPN) -  Tannase from Lactiplantibacillus plantarum

Seq: 469 a.a.

Struc: 452 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/j.jmb.2013.04.032

J Mol Biol 425:2737-2751 (2013)

PubMed id: 23648840

Crystal structure of tannase from Lactobacillus plantarum.

B.Ren, M.Wu, Q.Wang, X.Peng, H.Wen, W.J.McKinstry, Q.Chen.

ABSTRACT

Tannins are water-soluble polyphenolic compounds in plants. Hydrolyzable tannins are derivatives of gallic acid (3,4,5-trihydroxybenzoic acid) or its meta-depsidic forms that are esterified to polyol, catechin, or triterpenoid units. Tannases are a family of esterases that catalyze the hydrolysis of the galloyl ester bond in hydrolyzable tannins to release gallic acid. The enzymes have found wide applications in food, feed, beverage, pharmaceutical, and chemical industries since their discovery more than a century ago, although little is known about them at the molecular level, including the details of the catalytic and substrate binding sites. Here, we report the first three-dimensional structure of a tannase from Lactobacillus plantarum. The enzyme displays an α/β structure, featured by a large cap domain inserted into the classical serine hydrolase fold. A catalytic triad was identified in the structure, which is composed of Ser163, His451, and Asp419. During the binding of gallic acid, the carboxyl group of the molecule forges hydrogen-bonding interactions with the catalytic triad of the enzyme while the three hydroxyl groups make contacts with Asp421, Lys343, and Glu357 to form another hydrogen-bonding network. Mutagenesis studies demonstrated that these residues are indispensable for the activity of the enzyme. Structural studies of the enzyme in complex with a number of substrates indicated that the interactions at the galloyl binding site are the determinant force for the binding of substrates. The single galloyl binding site is responsible for the esterase and depsidase activities of the enzyme.