4IP2

Putative Aromatic Acid Decarboxylase

4IP2 の概要

• エントリーDOI: 10.2210/pdb4ip2/pdb
• 分子名称: Aromatic Acid Decarboxylase, MAGNESIUM ION, 1,2-ETHANEDIOL, ... (5 entities in total)
• 機能のキーワード: ubid-like decarboxylase, pa0254, huda, virulence attenuation factor, unknown function
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 171846.08

構造登録者

Schneider, G.,Brunner, K.,Izumi, A.,Jacewicz, A. (登録日: 2013-01-09, 公開日: 2013-07-10, 最終更新日: 2024-02-28)

主引用文献

Jacewicz, A.,Izumi, A.,Brunner, K.,Schnell, R.,Schneider, G.
Structural insights into the UbiD protein family from the crystal structure of PA0254 from Pseudomonas aeruginosa.
Plos One, 8:e63161-e63161, 2013

PubMed Abstract: The 3-polyprenyl-4-hydroxybenzoate decarboxylase (UbiD) catalyzes the conversion of 3-polyprenyl-4-hydroxybenzoate to 2-polyprenylphenol in the biosynthesis of ubiquinone. Pseudomonas aeruginosa contains two genes (PA0254 and PA5237) that are related in sequence to putative UbiD enzymes. A bioinformatics analysis suggests that the UbiD sequence family can be divided into two subclasses, with PA5237 and PA0254 belonging to different branches of this family. The three-dimensional structure of PA0254 has been determined using single wavelength anomalous diffraction and molecular replacement in two different crystal forms to resolutions of 1.95 and 2.3 Å, respectively. The subunit of PA0254 consists of three domains, an N-terminal α/β domain, a split β-barrel with a similar fold of a family of flavin reductases and a C-terminal α/β domain with a topology characteristic for the UbiD protein family. The middle domain contains a metal binding site adjacent to a large open cleft that may represent the active site. The two protein ligands binding a magnesium ion, His188 and Glu229, invariant in the PA0254 subclass, are also conserved in a corresponding metal site found in one of the FMN binding proteins from the split β-barrel fold family. PA0254 forms, in contrast to the hexameric UbiD from E. coli and P. aeruginosa, a homo-dimer. Insertion of four residues in a loop region in the PA0254 type enzymes results in structural differences that are incompatible with hexamer assembly.

PubMed: 23671667
DOI: 10.1371/journal.pone.0063161

実験手法

X-RAY DIFFRACTION (1.95 Å)