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2phh

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(New page: 200px<br /><applet load="2phh" size="450" color="white" frame="true" align="right" spinBox="true" caption="2phh, resolution 2.7&Aring;" /> '''THE COENZYME ANALOGUE...)
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[[Image:2phh.gif|left|200px]]<br /><applet load="2phh" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2phh, resolution 2.7&Aring;" />
 
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'''THE COENZYME ANALOGUE ADENOSINE 5-DIPHOSPHORIBOSE DISPLACES FAD IN THE ACTIVE SITE OF P-HYDROXYBENZOATE HYDROXYLASE. AN X-RAY CRYSTALLOGRAPHIC INVESTIGATION'''<br />
 
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==Overview==
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==THE COENZYME ANALOGUE ADENOSINE 5-DIPHOSPHORIBOSE DISPLACES FAD IN THE ACTIVE SITE OF P-HYDROXYBENZOATE HYDROXYLASE. AN X-RAY CRYSTALLOGRAPHIC INVESTIGATION==
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p-Hydroxybenzoate hydroxylase (PHBH) is an NADPH-dependent enzyme. To, locate the NADPH binding site, the enzyme was crystallized under anaerobic, conditions in the presence of the substrate p-hydroxybenzoate, the, coenzyme analogue adenosine 5-diphosphoribose (ADPR), and sodium, dithionite. This yielded colorless crystals that were suitable for X-ray, analysis. Diffraction data were collected up to 2.7-A resolution. A, difference Fourier between data from these colorless crystals and data, from yellow crystals of the enzyme-substrate complex showed that in the, colorless crystals the flavin ring was absent. The adenosine, 5'-diphosphate moiety, which is the common part between FAD and ADPR, was, still present. After restrained least-squares refinement of the, enzyme-substrate complex with the riboflavin omitted from the model, additional electron density appeared near the pyrophosphate, which, indicated the presence of an ADPR molecule in the FAD binding site of, PHBH. The complete ADPR molecule was fitted to the electron density, and, subsequent least-squares refinement resulted in a final R factor of 16.8%., Replacement of bound FAD by ADPR was confirmed by equilibrium dialysis, where it was shown that ADPR can effectively remove FAD from the enzyme, under mild conditions in 0.1 M potassium phosphate buffer, pH 8.0. The, empty pocket left by the flavin ring is filled by solvent, leaving the, architecture of the active site and the binding of the substrate largely, unaffected.
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<StructureSection load='2phh' size='340' side='right'caption='[[2phh]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2phh]] 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=2PHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PHH 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=APR:ADENOSINE-5-DIPHOSPHORIBOSE'>APR</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=2phh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2phh OCA], [https://pdbe.org/2phh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2phh RCSB], [https://www.ebi.ac.uk/pdbsum/2phh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2phh 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/ph/2phh_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=2phh 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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2PHH 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 APR 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=2PHH 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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The coenzyme analogue adenosine 5-diphosphoribose displaces FAD in the active site of p-hydroxybenzoate hydroxylase. An x-ray crystallographic investigation., van der Laan JM, Schreuder HA, Swarte MB, Wierenga RK, Kalk KH, Hol WG, Drenth J, Biochemistry. 1989 Sep 5;28(18):7199-205. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2819062 2819062]
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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: Drenth J]]
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[[Category: Derlaan, J.M.Van.]]
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[[Category: Hol WGJ]]
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[[Category: Drenth, J.]]
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[[Category: Van Derlaan JM]]
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[[Category: Hol, W.G.J.]]
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[[Category: APR]]
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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 Wed Nov 21 13:31:58 2007''
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Current revision

THE COENZYME ANALOGUE ADENOSINE 5-DIPHOSPHORIBOSE DISPLACES FAD IN THE ACTIVE SITE OF P-HYDROXYBENZOATE HYDROXYLASE. AN X-RAY CRYSTALLOGRAPHIC INVESTIGATION

PDB ID 2phh

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