1cc4

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(New page: 200px<br /><applet load="1cc4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cc4, resolution 2.0&Aring;" /> '''PHE161 AND ARG166 VAR...)
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[[Image:1cc4.gif|left|200px]]<br /><applet load="1cc4" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1cc4, resolution 2.0&Aring;" />
 
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'''PHE161 AND ARG166 VARIANTS OF P-HYDROXYBENZOATE HYDROXYLASE. IMPLICATIONS FOR NADPH RECOGNITION AND STRUCTURAL STABILITY.'''<br />
 
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==Overview==
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==PHE161 AND ARG166 VARIANTS OF P-HYDROXYBENZOATE HYDROXYLASE. IMPLICATIONS FOR NADPH RECOGNITION AND STRUCTURAL STABILITY.==
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Phe161 and Arg166 of p-hydroxybenzoate hydroxylase from Pseudomonas, fluorescens belong to a newly discovered sequence motif in flavoprotein, hydroxylases with a putative dual function in FAD and NADPH binding [1]., To study their role in more detail, Phe161 and Arg166 were selectively, changed by site-directed mutagenesis. F161A and F161G are catalytically, competent enzymes having a rather poor affinity for NADPH. The catalytic, properties of R166K are similar to those of the native enzyme. R166S and, R166E show impaired NADPH binding and R166E has lost the ability to bind, FAD. The crystal structure of substrate complexed F161A at 2.2 A is, indistinguishable from the native enzyme, except for small changes at the, site of mutation. The crystal structure of substrate complexed R166S at, 2.0 A revealed that Arg166 is important for providing an intimate contact, between the FAD binding domain and a long excursion of the substrate, binding domain. It is proposed that this interaction is essential for, structural stability and for the recognition of the pyrophosphate moiety, of NADPH.
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<StructureSection load='1cc4' size='340' side='right'caption='[[1cc4]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1cc4]] 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=1CC4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CC4 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&#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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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=1cc4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cc4 OCA], [https://pdbe.org/1cc4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cc4 RCSB], [https://www.ebi.ac.uk/pdbsum/1cc4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cc4 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/cc/1cc4_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=1cc4 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Phe161 and Arg166 of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens belong to a newly discovered sequence motif in flavoprotein hydroxylases with a putative dual function in FAD and NADPH binding [1]. To study their role in more detail, Phe161 and Arg166 were selectively changed by site-directed mutagenesis. F161A and F161G are catalytically competent enzymes having a rather poor affinity for NADPH. The catalytic properties of R166K are similar to those of the native enzyme. R166S and R166E show impaired NADPH binding and R166E has lost the ability to bind FAD. The crystal structure of substrate complexed F161A at 2.2 A is indistinguishable from the native enzyme, except for small changes at the site of mutation. The crystal structure of substrate complexed R166S at 2.0 A revealed that Arg166 is important for providing an intimate contact between the FAD binding domain and a long excursion of the substrate binding domain. It is proposed that this interaction is essential for structural stability and for the recognition of the pyrophosphate moiety of NADPH.
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==About this Structure==
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Phe161 and Arg166 variants of p-hydroxybenzoate hydroxylase. Implications for NADPH recognition and structural stability.,Eppink MH, Bunthol C, Schreuder HA, van Berkel WJ FEBS Lett. 1999 Jan 29;443(3):251-5. PMID:10025942<ref>PMID:10025942</ref>
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1CC4 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 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=1CC4 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Phe161 and Arg166 variants of p-hydroxybenzoate hydroxylase. Implications for NADPH recognition and structural stability., Eppink MH, Bunthol C, Schreuder HA, van Berkel WJ, FEBS Lett. 1999 Jan 29;443(3):251-5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10025942 10025942]
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</div>
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[[Category: 4-hydroxybenzoate 3-monooxygenase]]
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<div class="pdbe-citations 1cc4" style="background-color:#fffaf0;"></div>
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[[Category: Pseudomonas fluorescens]]
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[[Category: Single protein]]
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[[Category: Berkel, W.J.H.Van.]]
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[[Category: Bunthof, C.]]
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[[Category: Eppink, M.H.M.]]
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[[Category: Schreuder, H.A.]]
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[[Category: FAD]]
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[[Category: PHB]]
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[[Category: hydroxybenzoate]]
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[[Category: oxidoreductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:20:02 2007''
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==See Also==
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*[[Hydroxylases 3D structures|Hydroxylases 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Pseudomonas fluorescens]]
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[[Category: Bunthof C]]
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[[Category: Eppink MHM]]
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[[Category: Schreuder HA]]
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[[Category: Van Berkel WJH]]

Current revision

PHE161 AND ARG166 VARIANTS OF P-HYDROXYBENZOATE HYDROXYLASE. IMPLICATIONS FOR NADPH RECOGNITION AND STRUCTURAL STABILITY.

PDB ID 1cc4

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