2W2A: Crystal Structure Of P-Coumaric Acid Decarboxylase From Lactobacillus Plantarum: Structural Insights Into The Active Site And Decarboxylation Catalytic Mechanism

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.
PDB ID: 2W2ADownload
MMDB ID: 78120
PDB Deposition Date: 2008/10/27
Updated in MMDB: 2011/11
Experimental Method:
x-ray diffraction
Resolution: 1.38  Å
Source Organism:
Similar Structures:
Biological Unit for 2W2A: dimeric; determined by author and by software (PISA)
Molecular Components in 2W2A
Label Count Molecule
Proteins (2 molecules)
P-coumaric Acid Decarboxylase
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB