2WSJ

Crystal Structure of single point mutant Glu71Ser p-coumaric Acid Decarboxylase

2WSJ の概要

• エントリーDOI: 10.2210/pdb2wsj/pdb
• 関連するPDBエントリー: 2GC9 2W2A 2W2B 2W2F
• 分子名称: P-COUMARIC ACID DECARBOXYLASE, BARIUM ION, ISOPROPYL ALCOHOL, ... (6 entities in total)
• 機能のキーワード: catalytic mechanism, lactic acid, lyase
• 由来する生物種: LACTOBACILLUS PLANTARUM
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 42552.05

構造登録者

Rodriguez, H.,Angulo, I.,De Las Rivas, B.,Campillo, N.,Paez, J.A.,Munoz, R.,Mancheno, J.M. (登録日: 2009-09-07, 公開日: 2010-02-09, 最終更新日: 2023-12-20)

主引用文献

Rodriguez, H.,Angulo, I.,De Las Rivas, B.,Campillo, N.,Paez, J.A.,Munoz, R.,Mancheno, J.M.
P-Coumaric Acid Decarboxylase from Lactobacillus Plantarum: Structural Insights Into the Active Site and Decarboxylation Catalytic Mechanism.
Proteins, 78:1662-, 2010

PubMed 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.

PubMed: 20112419
DOI: 10.1002/PROT.22684

実験手法

X-RAY DIFFRACTION (2.24 Å)