1phh

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(New page: 200px<br /><applet load="1phh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1phh, resolution 2.3&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1phh.jpg|left|200px]]<br /><applet load="1phh" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1phh, resolution 2.3&Aring;" />
 
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'''CRYSTAL STRUCTURE OF P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH ITS REACTION PRODUCT 3,4-DIHYDROXYBENZOATE'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH ITS REACTION PRODUCT 3,4-DIHYDROXYBENZOATE==
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Crystals of the flavin-containing enzyme p-hydroxybenzoate hydroxylase, (PHBHase) complexed with its reaction product were investigated in order, to obtain insight into the catalytic cycle of this enzyme involving two, substrates and two cofactors. PHBHase was crystallized initially with its, substrate, p-hydroxybenzoate and the substrate was then converted into the, product 3,4-dihydroxybenzoate by allowing the catalytic reaction to, proceed in the crystals. In addition, crystals were soaked in mother, liquor containing a high concentration of this product. Data up to 2.3 A, (1 A = 0.1 nm) were collected by the oscillation method and the structure, of the enzyme product complex was refined by alternate restrained, least-squares procedures and model building by computer graphics, techniques. A total of 273 solvent molecules could be located, four of, them being presumably sulfate ions. The R-factor for 14,339 reflections, between 6.0 A and 2.3 A is 19.3%. The 3-hydroxyl group of the product, introduced by the enzyme is clearly visible in the electron density, showing unambiguously which carbon atom of the substrate is hydroxylated., A clear picture of the hydroxylation site is obtained. The plane of the, product is rotated 21 degrees with respect to the plane of the substrate, in the current model of enzyme-substrate complex. The 4-hydroxyl group of, the product is hydrogen bonded to the hydroxyl group of Tyr201, its, carboxyl group is interacting with the side-chains of Tyr222, Arg214 and, Ser212, while the newly introduced 3-hydroxyl group makes a hydrogen bond, with the backbone carbonyl oxygen of Pro293.
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<StructureSection load='1phh' size='340' side='right'caption='[[1phh]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1phh]] 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=1PHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PHH 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]] 2.3&#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=DHB:3,4-DIHYDROXYBENZOIC+ACID'>DHB</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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=1phh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1phh OCA], [https://pdbe.org/1phh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1phh RCSB], [https://www.ebi.ac.uk/pdbsum/1phh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1phh 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/1phh_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=1phh 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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1PHH 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 FAD and DHB 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=1PHH 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 complexed with its reaction product 3,4-dihydroxybenzoate., Schreuder HA, van der Laan JM, Hol WG, Drenth J, J Mol Biol. 1988 Feb 20;199(4):637-48. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=3351945 3351945]
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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: Drenth, J.]]
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[[Category: Schreuder HA]]
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[[Category: Schreuder, H.A.]]
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[[Category: DHB]]
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[[Category: FAD]]
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[[Category: oxidoreductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:49:09 2007''
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Current revision

CRYSTAL STRUCTURE OF P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH ITS REACTION PRODUCT 3,4-DIHYDROXYBENZOATE

PDB ID 1phh

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