6M53

Crystal structure of 2, 3-dihydroxybenzoic acid decarboxylase from Fusarium oxysporum

6M53 の概要

• エントリーDOI: 10.2210/pdb6m53/pdb
• 分子名称: 2,3-dihydroxybenzoate decarboxylase, ZINC ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: 2, 3-dihydroxybenzoic acid decarboxylase, biosynthetic protein
• 由来する生物種: Fusarium oxysporum (Fusarium vascular wilt)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 157699.47

構造登録者

Song, M.K.,Feng, J.H.,Liu, W.D.,Wu, Q.Q.,Zhu, D.M. (登録日: 2020-03-09, 公開日: 2020-07-15, 最終更新日: 2023-11-29)

主引用文献

Song, M.,Zhang, X.,Liu, W.,Feng, J.,Cui, Y.,Yao, P.,Wang, M.,Guo, R.T.,Wu, Q.,Zhu, D.
2,3-Dihydroxybenzoic Acid Decarboxylase from Fusarium oxysporum: Crystal Structures and Substrate Recognition Mechanism.
Chembiochem, 21:2950-2956, 2020

PubMed Abstract: A 2,3-dihydroxybenzoic acid decarboxylase from Fusarium oxysporum (2,3-DHBD_Fo) has a relatively high catalytic efficiency for the decarboxylation of 2,3-dihydroxybenzoic acid (DHBA) and carboxylation of catechol, thus it has a different substrate spectrum from other benzoic acid decarboxylases. We have determined the structures of 2,3-DHBD_Fo in its apo form and complexes with catechol or 2,5-dihydroxybenzoic acid at 1.55, 1.97, and 2.45 Å resolution, respectively. The crystal structures of 2,3-DHBD_Fo show that the enzyme exists as a homotetramer, and each active center has a Zn ion coordinated by E8, H167, D291 and three water molecules. This is different from 2,6-DHBD from Rhizobium sporomusa, in which the Zn ion is also coordinated with H10. Surprisingly, mutation of A10 of 2,3-DHBD_Fo to His resulted in almost complete loss of the enzyme activity. Enzyme-substrate docking and site-directed mutation studies indicate that residue R233 interacts with the 3-hydroxy group of 2,3-DHBA, and plays an important role in substrate recognition for this enzyme, thus revealing the molecular basis 2,3-dihydroxybenzoic acid decarboxylase.

PubMed: 32421914
DOI: 10.1002/cbic.202000244

実験手法

X-RAY DIFFRACTION (1.55 Å)