1oaf: Difference between revisions

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-[[Image:1oaf.gif|left|200px]]
- {{Structure
+==Ascobate peroxidase from soybean cytosol in complex with ascorbate==
-|PDB= 1oaf |SIZE=350|CAPTION= <scene name='initialview01'>1oaf</scene>, resolution 1.4&Aring;
+<StructureSection load='1oaf' size='340' side='right'caption='[[1oaf]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
-|SITE= <scene name='pdbsite=AC1:Asc+Binding+Site+For+Chain+A'>AC1</scene>
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=ASC:ASCORBIC+ACID'>ASC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>
+<table><tr><td colspan='2'>[[1oaf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OAF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OAF FirstGlance]. <br>
-|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/L-ascorbate_peroxidase L-ascorbate peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.11 1.11.1.11] </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]] 1.4&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASC:ASCORBIC+ACID'>ASC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=1oaf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oaf OCA], [https://pdbe.org/1oaf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oaf RCSB], [https://www.ebi.ac.uk/pdbsum/1oaf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oaf ProSAT]</span></td></tr>
-|RELATEDENTRY=
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oaf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oaf OCA], [http://www.ebi.ac.uk/pdbsum/1oaf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oaf RCSB]</span>
+== Function ==
-}}
+[https://www.uniprot.org/uniprot/Q43758_SOYBN Q43758_SOYBN]
+== 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/oa/1oaf_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=1oaf ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Heme peroxidases catalyze the H2O2-dependent oxidation of a variety of substrates, most of which are organic. Mechanistically, these enzymes are well characterized: they share a common catalytic cycle that involves formation of a two-electron, oxidized Compound I intermediate followed by two single-electron reduction steps by substrate. The substrate specificity is more diverse--most peroxidases oxidize small organic substrates, but there are prominent exceptions--and there is a notable absence of structural information for a representative peroxidase-substrate complex. Thus, the features that control substrate specificity remain undefined. We present the structure of the complex of ascorbate peroxidase-ascorbate. The structure defines the ascorbate-binding interaction for the first time and provides new rationalization of the unusual functional features of the related cytochrome c peroxidase enzyme, which has been a benchmark for peroxidase catalysis for more than 20 years. A new mechanism for electron transfer is proposed that challenges existing views of substrate oxidation in other peroxidases.
-'''ASCOBATE PEROXIDASE FROM SOYBEAN CYTOSOL IN COMPLEX WITH ASCORBATE'''
+Crystal structure of the ascorbate peroxidase-ascorbate complex.,Sharp KH, Mewies M, Moody PC, Raven EL Nat Struct Biol. 2003 Apr;10(4):303-7. PMID:12640445<ref>PMID:12640445</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1oaf" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-Heme peroxidases catalyze the H2O2-dependent oxidation of a variety of substrates, most of which are organic. Mechanistically, these enzymes are well characterized: they share a common catalytic cycle that involves formation of a two-electron, oxidized Compound I intermediate followed by two single-electron reduction steps by substrate. The substrate specificity is more diverse--most peroxidases oxidize small organic substrates, but there are prominent exceptions--and there is a notable absence of structural information for a representative peroxidase-substrate complex. Thus, the features that control substrate specificity remain undefined. We present the structure of the complex of ascorbate peroxidase-ascorbate. The structure defines the ascorbate-binding interaction for the first time and provides new rationalization of the unusual functional features of the related cytochrome c peroxidase enzyme, which has been a benchmark for peroxidase catalysis for more than 20 years. A new mechanism for electron transfer is proposed that challenges existing views of substrate oxidation in other peroxidases.
+*[[Ascorbate peroxidase|Ascorbate peroxidase]]
+*[[Ascorbate peroxidase 3D structures|Ascorbate peroxidase 3D structures]]
-==About this Structure==
+== References ==
-OAF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OAF OCA].
+<references/>
+__TOC__
-==Reference==
+</StructureSection>
-Crystal structure of the ascorbate peroxidase-ascorbate complex., Sharp KH, Mewies M, Moody PC, Raven EL, Nat Struct Biol. 2003 Apr;10(4):303-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12640445 12640445]
 [[Category: Glycine max]]
-[[Category: L-ascorbate peroxidase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Moody PCE]]
-[[Category: Moody, P C.E.]]
+[[Category: Raven EL]]
-[[Category: Raven, E L.]]
+[[Category: Sharp KH]]
-[[Category: Sharp, K H.]]
-[[Category: ascorbate peroxidase]]
-[[Category: heme peroxidase]]
-[[Category: peroxide scavenge]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:42:17 2008''