1ui8: Difference between revisions

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-[[Image:1ui8.gif|left|200px]]
- {{Structure
+==Site-directed mutagenesis of His592 involved in binding of copper ion in Arthrobacter globiformis amine oxidase==
-|PDB= 1ui8 |SIZE=350|CAPTION= <scene name='initialview01'>1ui8</scene>, resolution 1.8&Aring;
+<StructureSection load='1ui8' size='340' side='right'caption='[[1ui8]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=CU:COPPER (II) ION'>CU</scene>
+<table><tr><td colspan='2'>[[1ui8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arthrobacter_globiformis Arthrobacter globiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UI8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UI8 FirstGlance]. <br>
-|ACTIVITY= [http://en.wikipedia.org/wiki/Amine_oxidase_(copper-containing) Amine oxidase (copper-containing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.6 1.4.3.6]
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=TPQ:5-(2-CARBOXY-2-AMINOETHYL)-2-HYDROXY-1,4-BENZOQUINONE'>TPQ</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=1ui8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ui8 OCA], [https://pdbe.org/1ui8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ui8 RCSB], [https://www.ebi.ac.uk/pdbsum/1ui8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ui8 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PAOX_ARTGO PAOX_ARTGO]
+== 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/ui/1ui8_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=1ui8 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The topa quinone (TPQ) cofactor of copper amine oxidase is produced by posttranslational modification of a specific tyrosine residue through the copper-dependent, self-catalytic process. We have site-specifically mutated three histidine residues (His431, His433, and His592) involved in binding of the copper ion in the recombinant phenylethylamine oxidase from Arthrobacter globiformis. The mutant enzymes, in which each histidine was replaced by alanine, were purified in the Cu/TPQ-free precursor form and analyzed for their Cu-binding and TPQ-generating activities by UV-visible absorption, resonance Raman, and electron paramagnetic resonance spectroscopies. Among the three histidine-to-alanine mutants, only H592A was found to show a weak activity to form TPQ upon aerobic incubation with Cu(2+) ions. Also for H592A, exogenous imidazole rescued binding of copper and markedly promoted the TPQ formation. Accommodation of a free imidazole molecule within the cavity created in the active site of H592A was suggested by X-ray crystallography. Although the TPQ cofactor in H592A mutant was readily reduced with substrate, its catalytic activity was very low even in the presence of imidazole. Combined with the crystal structures of the mutant enzymes, these results demonstrate the importance of the three copper-binding histidine residues for both TPQ biogenesis and catalytic activity, fine-tuning the position of the essential metal.
-'''Site-directed mutagenesis of His592 involved in binding of copper ion in Arthrobacter globiformis amine oxidase'''
+Chemical rescue of a site-specific mutant of bacterial copper amine oxidase for generation of the topa quinone cofactor.,Matsunami H, Okajima T, Hirota S, Yamaguchi H, Hori H, Kuroda S, Tanizawa K Biochemistry. 2004 Mar 2;43(8):2178-87. PMID:14979714<ref>PMID:14979714</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1ui8" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-The topa quinone (TPQ) cofactor of copper amine oxidase is produced by posttranslational modification of a specific tyrosine residue through the copper-dependent, self-catalytic process. We have site-specifically mutated three histidine residues (His431, His433, and His592) involved in binding of the copper ion in the recombinant phenylethylamine oxidase from Arthrobacter globiformis. The mutant enzymes, in which each histidine was replaced by alanine, were purified in the Cu/TPQ-free precursor form and analyzed for their Cu-binding and TPQ-generating activities by UV-visible absorption, resonance Raman, and electron paramagnetic resonance spectroscopies. Among the three histidine-to-alanine mutants, only H592A was found to show a weak activity to form TPQ upon aerobic incubation with Cu(2+) ions. Also for H592A, exogenous imidazole rescued binding of copper and markedly promoted the TPQ formation. Accommodation of a free imidazole molecule within the cavity created in the active site of H592A was suggested by X-ray crystallography. Although the TPQ cofactor in H592A mutant was readily reduced with substrate, its catalytic activity was very low even in the presence of imidazole. Combined with the crystal structures of the mutant enzymes, these results demonstrate the importance of the three copper-binding histidine residues for both TPQ biogenesis and catalytic activity, fine-tuning the position of the essential metal.
+*[[Copper amine oxidase 3D structures|Copper amine oxidase 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-UI8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arthrobacter_globiformis Arthrobacter globiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UI8 OCA].
+__TOC__
+</StructureSection>
-==Reference==
-Chemical rescue of a site-specific mutant of bacterial copper amine oxidase for generation of the topa quinone cofactor., Matsunami H, Okajima T, Hirota S, Yamaguchi H, Hori H, Kuroda S, Tanizawa K, Biochemistry. 2004 Mar 2;43(8):2178-87. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14979714 14979714]
-[[Category: Amine oxidase (copper-containing)]]
 [[Category: Arthrobacter globiformis]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Hirota, S.]]
+[[Category: Hirota S]]
-[[Category: Hori, H.]]
+[[Category: Hori H]]
-[[Category: Kuroda, S.]]
+[[Category: Kuroda S]]
-[[Category: Matsunami, H.]]
+[[Category: Matsunami H]]
-[[Category: Okajima, T.]]
+[[Category: Okajima T]]
-[[Category: Tanizawa, K.]]
+[[Category: Tanizawa K]]
-[[Category: Yamaguchi, H.]]
+[[Category: Yamaguchi H]]
-[[Category: CU]]
-[[Category: amine oxidase]]
-[[Category: copper]]
-[[Category: histidine]]
-[[Category: metal coordination]]
-[[Category: oxidoreductase]]
-[[Category: quinone cofactor]]
-[[Category: tpq]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:32:20 2008''