PDBsum entry 2w2b

Lyase

PDB id: 2w2b

Contents

Protein chains

177 a.a. *

Ligands

ACT ×2

IPA ×2

Waters ×498

* Residue conservation analysis

PDB id:

2w2b

Name:

Lyase

Title:

Crystal structure of single point mutant tyr20phe p-coumaric acid decarboxylase from lactobacillus plantarum: structural insights into the active site and decarboxylation catalytic mechanism

Structure:

P-coumaric acid decarboxylase. Chain: a, b. Engineered: yes. Mutation: yes

Source:

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

Resolution:

1.40Å R-factor: 0.200 R-free: 0.221

Authors:

H.Rodriguez,I.Angulo,B.De Las Rivas,N.Campillo,J.A.Paez,R.Munoz, J.M.Mancheno

Key ref:

H.Rodríguez et al. (2010). p-Coumaric acid decarboxylase from Lactobacillus plantarum: structural insights into the active site and decarboxylation catalytic mechanism. Proteins, 78, 1662-1676. PubMed id: 20112419

Date:

27-Oct-08 Release date: 17-Nov-09

Protein chains

F9ULL2  (F9ULL2_LACPL) -  Phenolic acid decarboxylase from Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)

Seq: 178 a.a.

Struc: 177 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.4.1.1.- - ?????

Proteins 78:1662-1676 (2010)

PubMed id: 20112419

p-Coumaric acid decarboxylase from Lactobacillus plantarum: structural insights into the active site and decarboxylation catalytic mechanism.

H.Rodríguez, I.Angulo, B.de Las Rivas, N.Campillo, J.A.Páez, R.Muñoz, J.M.Mancheño.

ABSTRACT

p-Coumaric acid decarboxylases (PDCs) catalyze the nonoxidative decarboxylation of hydroxycinnamic acids to generate the corresponding vinyl derivatives. Despite the biotechnological relevance of PDCs in food industry, their catalytic mechanism remains largely unknown. Here, we report insights into the structural basis of catalysis for the homodimeric PDC from Lactobacillus plantarum (LpPDC). The global fold of LpPDC is based on a flattened beta-barrel surrounding an internal cavity. Crystallographic and functional analyses of single-point mutants of residues located within this cavity have permitted identifying a potential substrate-binding pocket and also to provide structural evidences for rearrangements of surface loops so that they can modulate the accessibility to the active site. Finally, combination of the structural and functional data with in silico results enables us to propose a two-step catalytic mechanism for decarboxylation of p-coumaric acid by PDCs where Glu71 is involved in proton transfer, and Tyr18 and Tyr20 are involved in the proper substrate orientation and in the release of the CO(2) product.