1foh

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(New page: 200px<br /><applet load="1foh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1foh, resolution 2.4&Aring;" /> '''PHENOL HYDROXYLASE FR...)
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[[Image:1foh.gif|left|200px]]<br /><applet load="1foh" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1foh, resolution 2.4&Aring;" />
 
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'''PHENOL HYDROXYLASE FROM TRICHOSPORON CUTANEUM'''<br />
 
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==Overview==
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==PHENOL HYDROXYLASE FROM TRICHOSPORON CUTANEUM==
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BACKGROUND: The synthesis of phenolic compounds as by-products of, industrial reactions poses a serious threat to the environment., Understanding the enzymatic reactions involved in the degradation and, detoxification of these compounds is therefore of much interest., Soil-living yeasts use flavin adenine dinucleotide (FAD)-containing, enzymes to hydroxylate phenols. This reaction initiates a metabolic, sequence permitting utilisation of the aromatic compound as a source of, carbon and energy. The phenol hydroxylase from Trichosporon cutaneum, hydroxylates phenol to catechol. Phenol is the best substrate, but the, enzyme also accepts simple hydroxyl-, amino-, halogen- or, methyl-substituted phenols. RESULTS: The crystal structure of phenol, hydroxylase in complex with FAD and phenol has been determined at 2.4 A, resolution. The structure was solved by the MIRAS method. The protein, model consists of two homodimers. The subunit consists of three domains, the first of which contains a beta sheet that binds FAD with a typical, beta alpha beta nucleotide-binding motif and also a fingerprint motif for, NADPH binding. The active site is located at the interface between the, first and second domains; the second domain also binds the phenolic, substrate. The third domain contains a thioredoxin-like fold and is, involved in dimer contacts. The subunits within the dimer show substantial, differences in structure and in FAD conformation. This conformational, flexibility allows the substrate to gain access to the active site and, excludes solvent during the hydroxylation reaction. CONCLUSIONS: Two of, the domains of phenol hydroxylase are similar in structure to, p-hydroxybenzoate hydroxylase. Thus, phenol hydroxylase is a member of a, family of flavin-containing aromatic hydroxylases that share the same, overall fold, in spite of large differences in amino acid sequences and, chain length. The structure of phenol hydroxylase is consistent with a, hydroxyl transfer mechanism via a peroxo-FAD intermediate. We propose that, a movement of FAD takes place in concert with a large conformational, change of residues 170-210 during catalysis.
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<StructureSection load='1foh' size='340' side='right'caption='[[1foh]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1foh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cutaneotrichosporon_cutaneum Cutaneotrichosporon cutaneum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FOH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FOH FirstGlance]. <br>
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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]] 2.4&#8491;</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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=IPH:PHENOL'>IPH</scene></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=1foh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1foh OCA], [https://pdbe.org/1foh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1foh RCSB], [https://www.ebi.ac.uk/pdbsum/1foh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1foh ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PHHY_CUTCT PHHY_CUTCT] Hydroxylates phenol to catechol (PubMed:1429434, PubMed:4146224, PubMed:3203745, PubMed:2022646, PubMed:7858421, PubMed:7851397, PubMed:11591156). Phenol is the best substrate, but the enzyme also accepts isomeric diphenols, hydroxyl-, amino-, halogen- or methyl-substituted phenols and, to a lesser degree, cresols (PubMed:4146224, PubMed:17425111, PubMed:7851397).<ref>PMID:11591156</ref> <ref>PMID:1429434</ref> <ref>PMID:17425111</ref> <ref>PMID:2022646</ref> <ref>PMID:3203745</ref> <ref>PMID:4146224</ref> <ref>PMID:7851397</ref> <ref>PMID:7858421</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fo/1foh_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1foh ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1FOH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Trichosporon_cutaneum Trichosporon cutaneum] with FAD and IPH as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phenol_2-monooxygenase Phenol 2-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.7 1.14.13.7] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FOH OCA].
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*[[Monooxygenase 3D structures|Monooxygenase 3D structures]]
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== References ==
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==Reference==
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<references/>
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The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis., Enroth C, Neujahr H, Schneider G, Lindqvist Y, Structure. 1998 May 15;6(5):605-17. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9634698 9634698]
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__TOC__
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[[Category: Phenol 2-monooxygenase]]
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</StructureSection>
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[[Category: Single protein]]
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[[Category: Cutaneotrichosporon cutaneum]]
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[[Category: Trichosporon cutaneum]]
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[[Category: Large Structures]]
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[[Category: Enroth, C.]]
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[[Category: Enroth C]]
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[[Category: Lindqvist, Y.]]
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[[Category: Lindqvist Y]]
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[[Category: Neujahr, H.]]
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[[Category: Neujahr H]]
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[[Category: Schneider, G.]]
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[[Category: Schneider G]]
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[[Category: FAD]]
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[[Category: IPH]]
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[[Category: flavin]]
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[[Category: monooxygenase]]
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[[Category: oxidoreductase]]
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[[Category: phenol hydroxylase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:05:36 2007''
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Current revision

PHENOL HYDROXYLASE FROM TRICHOSPORON CUTANEUM

PDB ID 1foh

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