3NAD

Crystal Structure of Phenolic Acid Decarboxylase from Bacillus pumilus UI-670

3NAD の概要

• エントリーDOI: 10.2210/pdb3nad/pdb
• 分子名称: Ferulate decarboxylase, SULFATE ION (3 entities in total)
• 機能のキーワード: beta barrel, lipocalin, biocatalysis, decarboxylase, lyase
• 由来する生物種: Bacillus pumilus (Bacillus mesentericus)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 38309.19

構造登録者

Matte, A.,Grosse, S.,Bergeron, H.,Abokitse, K.,Lau, P.C.K. (登録日: 2010-06-01, 公開日: 2010-11-10, 最終更新日: 2023-09-06)

主引用文献

Matte, A.,Grosse, S.,Bergeron, H.,Abokitse, K.,Lau, P.C.
Structural analysis of Bacillus pumilus phenolic acid decarboxylase, a lipocalin-fold enzyme.
Acta Crystallogr.,Sect.F, 66:1407-1414, 2010

PubMed Abstract: The decarboxylation of phenolic acids, including ferulic and p-coumaric acids, to their corresponding vinyl derivatives is of importance in the flavouring and polymer industries. Here, the crystal structure of phenolic acid decarboxylase (PAD) from Bacillus pumilus strain UI-670 is reported. The enzyme is a 161-residue polypeptide that forms dimers both in the crystal and in solution. The structure of PAD as determined by X-ray crystallography revealed a β-barrel structure and two α-helices, with a cleft formed at one edge of the barrel. The PAD structure resembles those of the lipocalin-fold proteins, which often bind hydrophobic ligands. Superposition of structurally related proteins bound to their cognate ligands shows that they and PAD bind their ligands in a conserved location within the β-barrel. Analysis of the residue-conservation pattern for PAD-related sequences mapped onto the PAD structure reveals that the conservation mainly includes residues found within the hydrophobic core of the protein, defining a common lipocalin-like fold for this enzyme family. A narrow cleft containing several conserved amino acids was observed as a structural feature and a potential ligand-binding site.

PubMed: 21045284
DOI: 10.1107/S174430911003246X

実験手法

X-RAY DIFFRACTION (1.69 Å)