5ZC2

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

Summary for 5ZC2

• Entry DOI: 10.2210/pdb5zc2/pdb
• Descriptor: p-hydroxyphenylacetate 3-hydroxylase, reductase component, FLAVIN MONONUCLEOTIDE (2 entities in total)
• Functional Keywords: flavin reductase, marr, flavoprotein
• Biological source: Acinetobacter baumannii
• Total number of polymer chains: 2
• Total formula weight: 71823.14

Authors

Yuenyao, A.,Petchyam, N.,Chaiyen, P.,Pakotiprapha, D. (deposition date: 2018-02-14, release date: 2018-08-08, Last modification date: 2024-03-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.898 Å)