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1pdh

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(New page: 200px<br /><applet load="1pdh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pdh, resolution 2.1&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1pdh.jpg|left|200px]]<br /><applet load="1pdh" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1pdh, resolution 2.1&Aring;" />
 
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'''CRYSTAL STRUCTURE OF P-HYDROXYBENZOATE HYDROXYLASE RECONSTITUTED WITH THE MODIFIED FAD PRESENT IN ALCOHOL OXIDASE FROM METHYLOTROPHIC YEASTS: EVIDENCE FOR AN ARABINOFLAVIN'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF P-HYDROXYBENZOATE HYDROXYLASE RECONSTITUTED WITH THE MODIFIED FAD PRESENT IN ALCOHOL OXIDASE FROM METHYLOTROPHIC YEASTS: EVIDENCE FOR AN ARABINOFLAVIN==
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The flavin prosthetic group (FAD) of p-hydroxybenzoate hydroxylase from, Pseudomonas fluorescens was replaced by a stereochemical analog, which is, spontaneously formed from natural FAD in alcohol oxidases from, methylotrophic yeasts. Reconstitution of p-hydroxybenzoate hydroxylase, from apoprotein and modified FAD is a rapid process complete within, seconds. Crystals of the enzyme-substrate complex of modified, FAD-containing p-hydroxybenzoate hydroxylase diffract to 2.1 A resolution., The crystal structure provides direct evidence for the presence of an, arabityl sugar chain in the modified form of FAD. The isoalloxazine ring, of the arabinoflavin adenine dinucleotide (a-FAD) is located in a cleft, outside the active site as recently observed in several other, p-hydroxybenzoate hydroxylase complexes. Like the native enzyme, a-FAD-containing p-hydroxybenzoate hydroxylase preferentially binds the, phenolate form of the substrate (pKo = 7.2). The substrate acts as an, effector highly stimulating the rate of enzyme reduction by NADPH (kred &gt;, 500 s-1). The oxidative part of the catalytic cycle of a-FAD-containing, p-hydroxybenzoate hydroxylase differs from native enzyme. Partial, uncoupling of hydroxylation results in the formation of about 0.3 mol of, 3,4-dihydroxybenzoate and 0.7 mol of hydrogen peroxide per mol NADPH, oxidized. It is proposed that flavin motion in p-hydroxybenzoate, hydroxylase is important for efficient reduction and that the flavin "out", conformation is associated with the oxidase activity.
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<StructureSection load='1pdh' size='340' side='right'caption='[[1pdh]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1pdh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PDH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PDH 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]] 2.1&#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=FAS:ARABINO-FLAVIN-ADENINE+DINUCLEOTIDE'>FAS</scene>, <scene name='pdbligand=PHB:P-HYDROXYBENZOIC+ACID'>PHB</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=1pdh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pdh OCA], [https://pdbe.org/1pdh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pdh RCSB], [https://www.ebi.ac.uk/pdbsum/1pdh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pdh ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PHHY_PSEFL PHHY_PSEFL]
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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/pd/1pdh_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=1pdh 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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1PDH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens] with FAS and PHB as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/4-hydroxybenzoate_3-monooxygenase 4-hydroxybenzoate 3-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.2 1.14.13.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PDH OCA].
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*[[Hydroxylases 3D structures|Hydroxylases 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of p-hydroxybenzoate hydroxylase reconstituted with the modified FAD present in alcohol oxidase from methylotrophic yeasts: evidence for an arabinoflavin., van Berkel WJ, Eppink MH, Schreuder HA, Protein Sci. 1994 Dec;3(12):2245-53. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7756982 7756982]
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[[Category: Large Structures]]
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[[Category: 4-hydroxybenzoate 3-monooxygenase]]
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[[Category: Pseudomonas fluorescens]]
[[Category: Pseudomonas fluorescens]]
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[[Category: Single protein]]
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[[Category: Eppink MHM]]
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[[Category: Berkel, W.J.H.Van.]]
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[[Category: Schreuder HA]]
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[[Category: Eppink, M.H.M.]]
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[[Category: Van Berkel WJH]]
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[[Category: Schreuder, H.A.]]
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[[Category: FAS]]
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[[Category: PHB]]
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[[Category: oxidoreductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:42:38 2007''
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Current revision

CRYSTAL STRUCTURE OF P-HYDROXYBENZOATE HYDROXYLASE RECONSTITUTED WITH THE MODIFIED FAD PRESENT IN ALCOHOL OXIDASE FROM METHYLOTROPHIC YEASTS: EVIDENCE FOR AN ARABINOFLAVIN

PDB ID 1pdh

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