1wa6

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[[Image:1wa6.png|left|200px]]
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==THE STRUCTURE OF ACC OXIDASE==
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<StructureSection load='1wa6' size='340' side='right' caption='[[1wa6]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1wa6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Petunia_x_hybrida Petunia x hybrida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WA6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WA6 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
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<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1w9y|1w9y]]</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aminocyclopropanecarboxylate_oxidase Aminocyclopropanecarboxylate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.17.4 1.14.17.4] </span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wa6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wa6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1wa6 RCSB], [http://www.ebi.ac.uk/pdbsum/1wa6 PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wa/1wa6_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The final step in the biosynthesis of the plant signaling molecule ethylene is catalyzed by 1-aminocyclopropane-1-carboxylic acid oxidase (ACCO). ACCO requires bicarbonate as an activator and catalyzes the oxidation of ACC to give ethylene, CO2, and HCN. We report crystal structures of ACCO in apo-form (2.1 A resolution) and complexed with Fe(II) (2.55 A) or Co(II) (2.4 A). The active site contains a single Fe(II) ligated by three residues (His177, Asp179, and His234), and it is relatively open compared to those of the 2-oxoglutarate oxygenases. The side chains of Arg175 and Arg244, proposed to be involved in binding bicarbonate, project away from the active site, but conformational changes may allow either or both to enter the active site. The structures will form a basis for future mechanistic and inhibition studies.
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{{STRUCTURE_1wa6| PDB=1wa6 | SCENE= }}
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Crystal structure and mechanistic implications of 1-aminocyclopropane-1-carboxylic acid oxidase--the ethylene-forming enzyme.,Zhang Z, Ren JS, Clifton IJ, Schofield CJ Chem Biol. 2004 Oct;11(10):1383-94. PMID:15489165<ref>PMID:15489165</ref>
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===THE STRUCTURE OF ACC OXIDASE===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_15489165}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1wa6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Petunia_x_hybrida Petunia x hybrida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WA6 OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:015489165</ref><references group="xtra"/>
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[[Category: Aminocyclopropanecarboxylate oxidase]]
[[Category: Aminocyclopropanecarboxylate oxidase]]
[[Category: Petunia x hybrida]]
[[Category: Petunia x hybrida]]

Revision as of 18:36, 29 September 2014

THE STRUCTURE OF ACC OXIDASE

1wa6, resolution 2.55Å

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