5ZC2

Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component (C1)

5ZC2 の概要

• エントリーDOI: 10.2210/pdb5zc2/pdb
• 分子名称: p-hydroxyphenylacetate 3-hydroxylase, reductase component, FLAVIN MONONUCLEOTIDE (2 entities in total)
• 機能のキーワード: flavin reductase, marr, flavoprotein
• 由来する生物種: Acinetobacter baumannii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 71823.14

構造登録者

Yuenyao, A.,Petchyam, N.,Chaiyen, P.,Pakotiprapha, D. (登録日: 2018-02-14, 公開日: 2018-08-08, 最終更新日: 2024-03-27)

主引用文献

Yuenyao, A.,Petchyam, N.,Kamonsutthipaijit, N.,Chaiyen, P.,Pakotiprapha, D.
Crystal structure of the flavin reductase of Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH) and identification of amino acid residues underlying its regulation by aromatic ligands
Arch. Biochem. Biophys., 653:24-38, 2018

PubMed Abstract: The first step in the degradation of p-hydroxyphenylacetic acid (HPA) is catalyzed by the two-component enzyme p-hydroxyphenylacetate 3-hydroxylase (HPAH). The two components of Acinetobacter baumannii HPAH are known as C and C, respectively. C is a flavin reductase that uses NADH to generate reduced flavin mononucleotide (FMNH), which is used by C in the hydroxylation of HPA. Interestingly, although HPA is not directly involved in the reaction catalyzed by C, the presence of HPA dramatically increases the FMN reduction rate. Amino acid sequence analysis revealed that C contains two domains: an N-terminal flavin reductase domain, and a C-terminal MarR domain. Although MarR proteins typically function as transcription regulators, the MarR domain of C was found to play an auto-inhibitory role. Here, we report a crystal structure of C and small-angle X-ray scattering (SAXS) studies that revealed that C undergoes a substantial conformational change in the presence of HPA, concomitant with the increase in the rate of flavin reduction. Amino acid residues that are important for HPA binding and regulation of C activity were identified by site-directed mutagenesis. Amino acid sequence similarity analysis revealed several as yet uncharacterized flavin reductases with N- or C-terminal fusions.

PubMed: 29940152
DOI: 10.1016/j.abb.2018.06.010

実験手法

X-RAY DIFFRACTION (2.898 Å)