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1aso

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X-RAY STRUCTURES AND MECHANISTIC IMPLICATIONS OF THREE FUNCTIONAL DERIVATIVES OF ASCORBATE OXIDASE FROM ZUCCHINI: REDUCED-, PEROXIDE-, AND AZIDE-FORMS

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Retrieved from "http://52.214.119.220/wiki/index.php/1aso"

Categories: Cucurbita pepo var. melopepo | Large Structures | Huber R | Luecke H | Messerschmidt A

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-[[Image:1aso.gif|left|200px]]<br /><applet load="1aso" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1aso, resolution 2.2&Aring;" />
-'''X-RAY STRUCTURES AND MECHANISTIC IMPLICATIONS OF THREE FUNCTIONAL DERIVATIVES OF ASCORBATE OXIDASE FROM ZUCCHINI: REDUCED-, PEROXIDE-, AND AZIDE-FORMS'''<br />
-==Overview==
+==X-RAY STRUCTURES AND MECHANISTIC IMPLICATIONS OF THREE FUNCTIONAL DERIVATIVES OF ASCORBATE OXIDASE FROM ZUCCHINI: REDUCED-, PEROXIDE-, AND AZIDE-FORMS==
-The X-ray structures of three functional derivatives of ascorbate oxidase, (EC 1.10.3.3) from Zucchini have been determined and are compared to the, "native" oxidized form. The fully reduced form of ascorbate oxidase has, been refined to a crystallographic R-factor of 19.6% for all reflections, between 8.0 A and 2.2 A resolution. The geometry at the type-1 copper, (CU1) is unchanged compared to the oxidized form, but the oxygen ligand, bridging the copper ions CU2 and CU3 (spectroscopic type-3 copper pair) is, released and the copper ions move apart yielding a trigonal planar, co-ordination with their ligating histidine residues. The co-ordination at, the copper ion CU4 (spectroscopic type-2 copper) is not affected. The, copper-copper distances increase from an average 3.7 A in the native form, to 5.1 A for CU2-CU3, 4.4 A for CU2-CU4 and 4.1 A for CU3-CU4. The, peroxide derivative of ascorbate oxidase has been refined to a, crystallographic R-factor of 16.0% for all reflections between 8.0 A and, 2.59 A resolution. The geometry at the type-1 copper site is not changed, compared to the oxidized form. The oxygen ligand bridging copper atoms CU2, and CU3 is lost, too. The peroxide binds terminally to the copper ion CU2, as hydroperoxide. Copper ion CU2 is fourfold co-ordinated to the NE2 atoms, of the three histidine residues and to the oxygen atom of the terminally, bound peroxide molecule in a distorted tetrahedral geometry. Copper ion, CU3 is threefold co-ordinated as in the reduced form and co-ordination, around copper atom CU4 is unaltered. The copper-copper distances increase, to 4.8 A for CU2-CU3 and 4.5 A for CU2-CU4. The distance CU3-CU4 remains, 3.7 A. Treatment with peroxide causes a partial depletion of copper ion, CU2. The refinement for the azide derivative of ascorbate oxidase, converged at a crystallographic R-factor of 17.8% for all reflections, between 8.0 A and 2.32 A. There are no significant structural changes at, the type-1 copper site. The oxygen ligand bridging copper ions CU2 and CU3, is again released. Two azide molecules bind terminally to copper ion CU2., Copper ion CU2 is fivefold co-ordinated to the NE2 atoms of the three, histidine residues and to both terminally bound azide molecules in a, trigonal-bipyramidal manner. Copper-copper distances increase to 5.1 A for, CU2-CU3 and 4.6 A for CU2-CU4. The distance CU3-CU4 is decreased to 3.6, A.(ABSTRACT TRUNCATED AT 400 WORDS)
+<StructureSection load='1aso' size='340' side='right'caption='[[1aso]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+== Structural highlights ==
-==About this Structure==
+<table><tr><td colspan='2'>[[1aso]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cucurbita_pepo_var._melopepo Cucurbita pepo var. melopepo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ASO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ASO FirstGlance]. <br>
-ASO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cucurbita_pepo_var._melopepo Cucurbita pepo var. melopepo] with NAG, CU and OH as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/L-ascorbate_oxidase L-ascorbate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.3.3 1.10.3.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ASO OCA].
+</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>
+<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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene></td></tr>
-==Reference==
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1aso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aso OCA], [https://pdbe.org/1aso PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aso RCSB], [https://www.ebi.ac.uk/pdbsum/1aso PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aso ProSAT]</span></td></tr>
-X-ray structures and mechanistic implications of three functional derivatives of ascorbate oxidase from zucchini. Reduced, peroxide and azide forms., Messerschmidt A, Luecke H, Huber R, J Mol Biol. 1993 Apr 5;230(3):997-1014. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8478945 8478945]
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ASO_CUCPM ASO_CUCPM] May be involved in a redox system involving ascorbic acid.
+== 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/as/1aso_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=1aso ConSurf].
+<div style="clear:both"></div>
+__TOC__
+</StructureSection>
 [[Category: Cucurbita pepo var. melopepo]]
-[[Category: L-ascorbate oxidase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Huber R]]
-[[Category: Huber, R.]]
+[[Category: Luecke H]]
-[[Category: Luecke, H.]]
+[[Category: Messerschmidt A]]
-[[Category: Messerschmidt, A.]]
-[[Category: CU]]
-[[Category: NAG]]
-[[Category: OH]]
-[[Category: oxidoreductase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:06:28 2007''

1aso

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X-RAY STRUCTURES AND MECHANISTIC IMPLICATIONS OF THREE FUNCTIONAL DERIVATIVES OF ASCORBATE OXIDASE FROM ZUCCHINI: REDUCED-, PEROXIDE-, AND AZIDE-FORMS

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Evolutionary Conservation

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