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PDBsum entry 4j0j

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
4j0j
Jmol
Contents
Protein chains
470 a.a.
Ligands
E35 ×2
Waters ×501
PDB id:
4j0j
Name: Hydrolase
Title: Tannin acyl hydrolase in complex with ethyl 3,5-dihydroxyben
Structure: Tannase. Chain: a, b. Engineered: yes
Source: Lactobacillus plantarum. Organism_taxid: 1590. Gene: tanlpl. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.00Å     R-factor:   0.186     R-free:   0.217
Authors: B.Ren,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:
31-Jan-13     Release date:   22-May-13    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam  
B3Y018  (B3Y018_LACPN) -  Tannase
Seq:
Struc:
469 a.a.
470 a.a.
Key:    Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     metal ion binding     1 term  

 

 
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.