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<StructureSection load='2phh' size='340' side='right'caption='[[2phh]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='2phh' size='340' side='right'caption='[[2phh]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2phh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_liquefaciens"_flugge_1886 "bacillus fluorescens liquefaciens" flugge 1886]. 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 [http://proteopedia.org/fgij/fg.htm?mol=2PHH FirstGlance]. <br>
<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>
</td></tr><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>
</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>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2phh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2phh OCA], [http://pdbe.org/2phh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2phh RCSB], [http://www.ebi.ac.uk/pdbsum/2phh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2phh ProSAT]</span></td></tr>
<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>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PHHY_PSEFL PHHY_PSEFL]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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].
</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].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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:2819062<ref>PMID:2819062</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2phh" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Hydroxylases 3D structures|Hydroxylases 3D structures]]
*[[Hydroxylases 3D structures|Hydroxylases 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus fluorescens liquefaciens flugge 1886]]
[[Category: 4-hydroxybenzoate 3-monooxygenase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Derlaan, J M.Van]]
[[Category: Pseudomonas fluorescens]]
[[Category: Drenth, J]]
[[Category: Drenth J]]
[[Category: Hol, W G.J]]
[[Category: Hol WGJ]]
[[Category: Oxidoreductase]]
[[Category: Van Derlaan JM]]

Latest revision as of 12:09, 21 February 2024

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

Structural highlights

2phh is a 1 chain structure with sequence from Pseudomonas fluorescens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PHHY_PSEFL

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2phh, resolution 2.70Å

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