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1dod

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(New page: 200px<br /><applet load="1dod" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dod, resolution 2.1&Aring;" /> '''THE MOBIL FLAVIN OF 4...)
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[[Image:1dod.gif|left|200px]]<br /><applet load="1dod" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1dod, resolution 2.1&Aring;" />
 
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'''THE MOBIL FLAVIN OF 4-OH BENZOATE HYDROXYLASE: MOTION OF A PROSTHETIC GROUP REGULATES CATALYSIS'''<br />
 
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==Overview==
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==THE MOBIL FLAVIN OF 4-OH BENZOATE HYDROXYLASE: MOTION OF A PROSTHETIC GROUP REGULATES CATALYSIS==
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Para-hydroxybenzoate hydroxylase inserts oxygen into substrates by means, of the labile intermediate, flavin C(4a)-hydroperoxide. This reaction, requires transient isolation of the flavin and substrate from the bulk, solvent. Previous crystal structures have revealed the position of the, substrate para-hydroxybenzoate during oxygenation but not how it enters, the active site. In this study, enzyme structures with the flavin ring, displaced relative to the protein were determined, and it was established, that these or similar flavin conformations also occur in solution., Movement of the flavin appears to be essential for the translocation of, substrates and products into the solvent-shielded active site during, catalysis.
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<StructureSection load='1dod' size='340' side='right'caption='[[1dod]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1dod]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DOD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DOD 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=DOB:2,4-DIHYDROXYBENZOIC+ACID'>DOB</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=1dod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dod OCA], [https://pdbe.org/1dod PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dod RCSB], [https://www.ebi.ac.uk/pdbsum/1dod PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dod ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PHHY_PSEAE PHHY_PSEAE]
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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/do/1dod_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=1dod 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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1DOD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with FAD and DOB as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DOD 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 mobile flavin of 4-OH benzoate hydroxylase., Gatti DL, Palfey BA, Lah MS, Entsch B, Massey V, Ballou DP, Ludwig ML, Science. 1994 Oct 7;266(5182):110-4. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7939628 7939628]
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[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
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[[Category: Single protein]]
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[[Category: Ballou DP]]
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[[Category: Ballou, D.P.]]
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[[Category: Entsch B]]
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[[Category: Entsch, B.]]
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[[Category: Gatti DL]]
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[[Category: Gatti, D.L.]]
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[[Category: Lah MS]]
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[[Category: Lah, M.S.]]
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[[Category: Ludwig ML]]
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[[Category: Ludwig, M.L.]]
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[[Category: Massey V]]
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[[Category: Massey, V.]]
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[[Category: Palfey BA]]
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[[Category: Palfey, B.A.]]
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[[Category: DOB]]
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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 13:26:43 2007''
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Current revision

THE MOBIL FLAVIN OF 4-OH BENZOATE HYDROXYLASE: MOTION OF A PROSTHETIC GROUP REGULATES CATALYSIS

PDB ID 1dod

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