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1ahu

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[[Image:1ahu.gif|left|200px]]<br />
 
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<applet load="1ahu" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ahu, resolution 2.7&Aring;" />
 
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'''STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH P-CRESOL'''<br />
 
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==Overview==
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==STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH P-CRESOL==
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BACKGROUND: Lignin degradation leads to the formation of a broad spectrum, of aromatic molecules that can be used by various fungal micro-organisms, as their sole source of carbon. When grown on phenolic compounds, Penicillium simplicissimum induces the strong impression of a, flavin-containing vanillyl-alcohol oxidase (VAO). The enzyme catalyses the, oxidation of a vast array of substrates, ranging from aromatic amines to, 4-alkyphenols. VAO is a member of a novel class of widely distributed, oxidoreductases, which use flavin adenine dinucleotide (FAD) as a cofactor, covalently bound to the protein. We have carried out the determination of, the structure of VAO in order to shed light on the most interesting, features of these novel oxidoreductases, such as the functional, significance of ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9261083 (full description)]]
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<StructureSection load='1ahu' size='340' side='right'caption='[[1ahu]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ahu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Penicillium_simplicissimum Penicillium simplicissimum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AHU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AHU 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]] 2.7&#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=FAA:N5-(4-HYDROXYBENZYL)FLAVIN-ADENINE+DINUCLEOTIDE'>FAA</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=1ahu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ahu OCA], [https://pdbe.org/1ahu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ahu RCSB], [https://www.ebi.ac.uk/pdbsum/1ahu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ahu ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/VAOX_PENSI VAOX_PENSI] Catalyzes the conversion of vanillin alcohol to vanillin, and also the conversion of a wide range of phenolic compounds bearing side chains of variable size at the para position of the aromatic ring. Crucial for the degradation of the secondary metabolites derived from the degradation of the lignin. Catalyzes besides the oxidation of 4-hydroxybenzyl alcohols, the oxidative deamination of 4-hydroxybenzylamines, the oxidative demethylation of 4-(methoxy-methyl)phenols and the oxidative hydration of 4-allylphenols. Most active with 4-allylphenols.
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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/ah/1ahu_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=1ahu 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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1AHU is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Penicillium_simplicissimum Penicillium simplicissimum]] with FAA as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Alcohol_oxidase Alcohol oxidase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.13 1.1.3.13]]. Structure known Active Site: FAA. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AHU OCA]].
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*[[Vanillyl-alcohol oxidase|Vanillyl-alcohol oxidase]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: the shape of the active-site cavity controls substrate specificity., Mattevi A, Fraaije MW, Mozzarelli A, Olivi L, Coda A, van Berkel WJ, Structure. 1997 Jul 15;5(7):907-20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9261083 9261083]
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[[Category: Large Structures]]
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[[Category: Alcohol oxidase]]
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[[Category: Penicillium simplicissimum]]
[[Category: Penicillium simplicissimum]]
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[[Category: Single protein]]
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[[Category: Mattevi A]]
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[[Category: Mattevi, A.]]
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[[Category: FAA]]
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[[Category: catalysis]]
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[[Category: flavoenzyme]]
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[[Category: oxidase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:48:22 2007''
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Current revision

STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH P-CRESOL

PDB ID 1ahu

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