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[[Image:2bix.gif|left|200px]]


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==Crystal structure of apocarotenoid cleavage oxygenase from Synechocystis, Fe-free apoenzyme==
The line below this paragraph, containing "STRUCTURE_2bix", creates the "Structure Box" on the page.
<StructureSection load='2bix' size='340' side='right'caption='[[2bix]], [[Resolution|resolution]] 2.68&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2bix]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BIX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BIX FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.68&#8491;</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
{{STRUCTURE_2bix| PDB=2bix  | SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bix FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bix OCA], [https://pdbe.org/2bix PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bix RCSB], [https://www.ebi.ac.uk/pdbsum/2bix PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bix ProSAT]</span></td></tr>
 
</table>
'''CRYSTAL STRUCTURE OF APOCAROTENOID CLEAVAGE OXYGENASE FROM SYNECHOCYSTIS, FE-FREE APOENZYME'''
== Function ==
 
[https://www.uniprot.org/uniprot/ACOX_SYNY3 ACOX_SYNY3] Cleaves a number of carotenals and carotenols in the all-trans configuration at the 15-15' double bond producing retinal or retinol, respectively. Also shows activity toward lycopenals and the corresponding alcohols. Does not cleave beta-carotene or lycopene.
 
== Evolutionary Conservation ==
==Overview==
[[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/bi/2bix_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=2bix ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Enzymes that produce retinal and related apocarotenoids constitute a sequence- and thus structure-related family, a member of which was analyzed by x-ray diffraction. This member is an oxygenase and contains an Fe2+-4-His arrangement at the axis of a seven-bladed beta-propeller chain fold covered by a dome formed by six large loops. The Fe2+ is accessible through a long nonpolar tunnel that holds a carotenoid derivative in one of the crystals. On binding, three consecutive double bonds of this carotenoid changed from a straight all-trans to a cranked cis-trans-cis conformation. The remaining trans bond is located at the dioxygen-ligated Fe2+ and cleaved by oxygen.
Enzymes that produce retinal and related apocarotenoids constitute a sequence- and thus structure-related family, a member of which was analyzed by x-ray diffraction. This member is an oxygenase and contains an Fe2+-4-His arrangement at the axis of a seven-bladed beta-propeller chain fold covered by a dome formed by six large loops. The Fe2+ is accessible through a long nonpolar tunnel that holds a carotenoid derivative in one of the crystals. On binding, three consecutive double bonds of this carotenoid changed from a straight all-trans to a cranked cis-trans-cis conformation. The remaining trans bond is located at the dioxygen-ligated Fe2+ and cleaved by oxygen.


==About this Structure==
The structure of a retinal-forming carotenoid oxygenase.,Kloer DP, Ruch S, Al-Babili S, Beyer P, Schulz GE Science. 2005 Apr 8;308(5719):267-9. PMID:15821095<ref>PMID:15821095</ref>
2BIX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BIX OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
The structure of a retinal-forming carotenoid oxygenase., Kloer DP, Ruch S, Al-Babili S, Beyer P, Schulz GE, Science. 2005 Apr 8;308(5719):267-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15821095 15821095]
</div>
[[Category: Single protein]]
<div class="pdbe-citations 2bix" style="background-color:#fffaf0;"></div>
[[Category: Synechocystis sp.]]
== References ==
[[Category: Al-Babili, S.]]
<references/>
[[Category: Beyer, P.]]
__TOC__
[[Category: Kloer, D P.]]
</StructureSection>
[[Category: Ruch, S.]]
[[Category: Large Structures]]
[[Category: Schulz, G E.]]
[[Category: Synechocystis sp. PCC 6803]]
[[Category: Carotenoid cleavage]]
[[Category: Al-Babili S]]
[[Category: Dioxygenase]]
[[Category: Beyer P]]
[[Category: Non-heme iron]]
[[Category: Kloer DP]]
[[Category: Oxidoreductase]]
[[Category: Ruch S]]
[[Category: Oxygenase]]
[[Category: Schulz GE]]
[[Category: Retinal formation]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 20:21:15 2008''

Latest revision as of 09:16, 9 May 2024

Crystal structure of apocarotenoid cleavage oxygenase from Synechocystis, Fe-free apoenzyme

2bix, resolution 2.68Å

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