1dod: Difference between revisions

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 ==THE MOBIL FLAVIN OF 4-OH BENZOATE HYDROXYLASE: MOTION OF A PROSTHETIC GROUP REGULATES CATALYSIS==
-<StructureSection load='1dod' size='340' side='right' caption='[[1dod]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+<StructureSection load='1dod' size='340' side='right'caption='[[1dod]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1dod]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DOD FirstGlance]. <br>
+<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>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DOB:2,4-DIHYDROXYBENZOIC+ACID'>DOB</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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]] 2.1&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dod OCA], [http://pdbe.org/1dod PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dod RCSB], [http://www.ebi.ac.uk/pdbsum/1dod PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1dod ProSAT]</span></td></tr>
+<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>
+<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>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/PHHY_PSEAE PHHY_PSEAE]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/do/1dod_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/do/1dod_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 17: / Line 20: @@
 </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].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-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.
-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:7939628<ref>PMID:7939628</ref>
+==See Also==
+*[[Hydroxylases 3D structures|Hydroxylases 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1dod" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Ballou, D P]]
+[[Category: Large Structures]]
-[[Category: Entsch, B]]
+[[Category: Pseudomonas aeruginosa]]
-[[Category: Gatti, D L]]
+[[Category: Ballou DP]]
-[[Category: Lah, M S]]
+[[Category: Entsch B]]
-[[Category: Ludwig, M L]]
+[[Category: Gatti DL]]
-[[Category: Massey, V]]
+[[Category: Lah MS]]
-[[Category: Palfey, B A]]
+[[Category: Ludwig ML]]
-[[Category: Oxidoreductase]]
+[[Category: Massey V]]
+[[Category: Palfey BA]]