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- SASDD64: p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant... -
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Basic information
Entry | ![]() |
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![]() | p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 8 mg/ml of H170A C1 in 1 mM of p-hydroxyphenylacetic acid (HPA)
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Biological species | ![]() |
![]() | ![]() 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. |
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Structure visualization
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-Data source
SASBDB page | ![]() |
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-Related structure data
-Models
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Sample
![]() | Name: p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 8 mg/ml of H170A C1 in 1 mM of p-hydroxyphenylacetic acid (HPA) Specimen concentration: 8 mg/ml |
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Buffer | Name: 50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, 5% glycerol, 1 mM HPA pH: 7 |
Entity #982 | Name: H170A C1 reductase / Type: protein Description: p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component H170A mutant Formula weight: 35.346 / Num. of mol.: 2 / Source: Acinetobacter baumannii Sequence: MNQLNTAIVE KEVIDPMAFR RALGNFATGV TIMTAQTSSG ERVGVTANSF NSVSLDPALV LWSIDKKSSS YRIFEEATHF GVNILSAAQI ELSNRFARRS EDKFANIEFD LGVGNIPLFK NCSAAFECER YNIVEGGDHW IIIGRVVKFH DHGRSPLLYH QGAYSAVLPA ...Sequence: MNQLNTAIVE KEVIDPMAFR RALGNFATGV TIMTAQTSSG ERVGVTANSF NSVSLDPALV LWSIDKKSSS YRIFEEATHF GVNILSAAQI ELSNRFARRS EDKFANIEFD LGVGNIPLFK NCSAAFECER YNIVEGGDHW IIIGRVVKFH DHGRSPLLYH QGAYSAVLPA PSLNMKSETA EGVFPGRLYD NMYYLLTQAV RAYQNDYQPK QLASGFRTSE ARLLLVLESK TASSKCDLQR EVAMPIREIE EATKILSEKG LLIDNGQHYE LTEQGNACAH MLYKIAESHQ EEVFAKYTVD ERKLFKNMLK DLIGI |
-Experimental information
Beam | Instrument name: Synchrotron Light Research Institute (SLRI) BL1.3W City: Nakhon Ratchasima / 国: Thailand ![]() | ||||||||||||||||||||||||||||||
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Detector | Name: Rayonix SX165 / Type: CCD / Pixsize x: 15 mm | ||||||||||||||||||||||||||||||
Scan | Measurement date: Mar 7, 2017 / Storage temperature: 4 °C / Cell temperature: 16 °C / Exposure time: 600 sec. / Number of frames: 1 / Unit: 1/A /
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Distance distribution function P(R) |
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Result |
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