1ius: Difference between revisions

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-[[Image:1ius.gif|left|200px]]
- {{Structure
+==P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-AMINOBENZOATE AT PH 5.0==
-|PDB= 1ius |SIZE=350|CAPTION= <scene name='initialview01'>1ius</scene>, resolution 2.2&Aring;
+<StructureSection load='1ius' size='340' side='right'caption='[[1ius]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PAB:4-AMINOBENZOIC+ACID'>PAB</scene>
+<table><tr><td colspan='2'>[[1ius]] 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=1IUS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IUS FirstGlance]. <br>
-|ACTIVITY= <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
-|GENE=
+<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=PAB:4-AMINOBENZOIC+ACID'>PAB</scene></td></tr>
-|DOMAIN=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ius FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ius OCA], [https://pdbe.org/1ius PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ius RCSB], [https://www.ebi.ac.uk/pdbsum/1ius PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ius ProSAT]</span></td></tr>
-|RELATEDENTRY=
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ius FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ius OCA], [http://www.ebi.ac.uk/pdbsum/1ius PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ius RCSB]</span>
+== 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/iu/1ius_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1ius ConSurf].
+<div style="clear:both"></div>
-'''P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-AMINOBENZOATE AT PH 5.0'''
+==See Also==
+*[[Hydroxylases 3D structures|Hydroxylases 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-Deprotonation of p-hydroxybenzoate to the phenolate and reprotonation of the hydroxylated dienone intermediate to form the product are essential steps in the reaction catalyzed by p-hydroxybenzoate hydroxylase (PHBH). The mechanism by which protons are transferred in these reactions is not obvious, because the substrate bound in the active site is isolated from solvent. Structure analyses of wild-type and mutant PHBH, with bound p-hydroxybenzoate or p-aminobenzoate, reveal a chain of proton donors and acceptors (the hydroxyl groups of Tyr201 and Tyr385, and two water molecules) that can connect the substrate 4-OH to His72, a surface residue. This chain could provide a pathway for proton transfer to and from the substrate. Using various combinations of pH and substrates, we show that in crystalline PHBH ionizable groups in the chain may rotate and change hydrogen-bond orientation. Molecular dynamics simulations have been used to predict the preferred orientation of hydrogen bonds in the chain as a function of the ionization states of substrate and His72. The calculations suggest that changes in the ionization state of the substrate could be associated with changes in orientation of the hydrogen bonds in the chain. Transfer of water between the chain of proton donors and the solvent also appears to be an essential part of the mechanism that provides reversible transfer of protons during the hydroxylation reaction.
+[[Category: Large Structures]]
-==About this Structure==
-IUS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IUS OCA].
-==Reference==
-pH-dependent structural changes in the active site of p-hydroxybenzoate hydroxylase point to the importance of proton and water movements during catalysis., Gatti DL, Entsch B, Ballou DP, Ludwig ML, Biochemistry. 1996 Jan 16;35(2):567-78. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8555229 8555229]
-[[Category: 4-hydroxybenzoate 3-monooxygenase]]
 [[Category: Pseudomonas aeruginosa]]
-[[Category: Single protein]]
+[[Category: Ballou DP]]
-[[Category: Ballou, D P.]]
+[[Category: Entsch B]]
-[[Category: Entsch, B.]]
+[[Category: Gatti DL]]
-[[Category: Gatti, D L.]]
+[[Category: Ludwig ML]]
-[[Category: Ludwig, M L.]]
-[[Category: oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:24:56 2008''