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Yorodumi- PDB-5zc2: Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPA... -
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-Basic information
Entry | Database: PDB / ID: 5zc2 | |||||||||
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Title | Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component (C1) | |||||||||
Components | p-hydroxyphenylacetate 3-hydroxylase, reductase component | |||||||||
Keywords | FLAVOPROTEIN / Flavin reductase / MarR | |||||||||
Function / homology | Function and homology information flavin reductase (NADH) / flavin reductase (NADH) activity / riboflavin reductase (NADPH) activity / : / FMN binding Similarity search - Function | |||||||||
Biological species | Acinetobacter baumannii (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.898 Å | |||||||||
Authors | Yuenyao, A. / Petchyam, N. / Chaiyen, P. / Pakotiprapha, D. | |||||||||
Funding support | Thailand, 2items
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Citation | Journal: Arch Biochem Biophys / Year: 2018 Title: 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. Authors: Anan Yuenyao / Nopphon Petchyam / Nuntaporn Kamonsutthipaijit / Pimchai Chaiyen / Danaya Pakotiprapha / 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 ...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. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
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PDBx/mmCIF format | 5zc2.cif.gz | 241.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5zc2.ent.gz | 196.5 KB | Display | PDB format |
PDBx/mmJSON format | 5zc2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5zc2_validation.pdf.gz | 1 MB | Display | wwPDB validaton report |
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Full document | 5zc2_full_validation.pdf.gz | 1 MB | Display | |
Data in XML | 5zc2_validation.xml.gz | 22.5 KB | Display | |
Data in CIF | 5zc2_validation.cif.gz | 29.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zc/5zc2 ftp://data.pdbj.org/pub/pdb/validation_reports/zc/5zc2 | HTTPS FTP |
-Related structure data
Related structure data | C: citing same article (ref.) |
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Similar structure data | |
Other databases |
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-Links
-Assembly
Deposited unit |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Ens-ID: 1
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