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5zc2

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Current revision (10:27, 27 March 2024) (edit) (undo)
 
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<StructureSection load='5zc2' size='340' side='right'caption='[[5zc2]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='5zc2' size='340' side='right'caption='[[5zc2]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5zc2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZC2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ZC2 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5zc2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii Acinetobacter baumannii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZC2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZC2 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.898&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Flavin_reductase_(NADH) Flavin reductase (NADH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.36 1.5.1.36] </span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5zc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zc2 OCA], [http://pdbe.org/5zc2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zc2 RCSB], [http://www.ebi.ac.uk/pdbsum/5zc2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zc2 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5zc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zc2 OCA], [https://pdbe.org/5zc2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zc2 RCSB], [https://www.ebi.ac.uk/pdbsum/5zc2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zc2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/HPAHR_ACIBA HPAHR_ACIBA]] Reductase component of a two-component system that supplies reduced FMN (FMNH2) to the oxygenase component to catalyze the hydroxylation of 4-hydroxyphenylacetic acid, leading to the production of 3,4-dihydroxyphenylacetate (3,4-DHPA). Catalyzes the reduction of free flavins (FMN, FAD and riboflavin) by NADH. Subsequently, the reduced flavins diffuse to the oxygenase component C2.<ref>PMID:11683878</ref> <ref>PMID:16042421</ref> <ref>PMID:17595116</ref>
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[https://www.uniprot.org/uniprot/HPAHR_ACIBA HPAHR_ACIBA] Reductase component of a two-component system that supplies reduced FMN (FMNH2) to the oxygenase component to catalyze the hydroxylation of 4-hydroxyphenylacetic acid, leading to the production of 3,4-dihydroxyphenylacetate (3,4-DHPA). Catalyzes the reduction of free flavins (FMN, FAD and riboflavin) by NADH. Subsequently, the reduced flavins diffuse to the oxygenase component C2.<ref>PMID:11683878</ref> <ref>PMID:16042421</ref> <ref>PMID:17595116</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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 C1 and C2, respectively. C1 is a flavin reductase that uses NADH to generate reduced flavin mononucleotide (FMNH(-)), which is used by C2 in the hydroxylation of HPA. Interestingly, although HPA is not directly involved in the reaction catalyzed by C1, the presence of HPA dramatically increases the FMN reduction rate. Amino acid sequence analysis revealed that C1 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 C1 was found to play an auto-inhibitory role. Here, we report a crystal structure of C1 and small-angle X-ray scattering (SAXS) studies that revealed that C1 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 C1 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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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.,Yuenyao A, Petchyam N, Kamonsutthipaijit N, Chaiyen P, Pakotiprapha D Arch Biochem Biophys. 2018 Jun 22;653:24-38. doi: 10.1016/j.abb.2018.06.010. PMID:29940152<ref>PMID:29940152</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5zc2" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Acinetobacter baumannii]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chaiyen, P]]
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[[Category: Chaiyen P]]
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[[Category: Pakotiprapha, D]]
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[[Category: Pakotiprapha D]]
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[[Category: Petchyam, N]]
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[[Category: Petchyam N]]
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[[Category: Yuenyao, A]]
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[[Category: Yuenyao A]]
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[[Category: Flavin reductase]]
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[[Category: Flavoprotein]]
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[[Category: Marr]]
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Current revision

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

PDB ID 5zc2

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