2biw

==CRYSTAL STRUCTURE OF APOCAROTENOID CLEAVAGE OXYGENASE FROM SYNECHOCYSTIS, NATIVE ENZYME==

<StructureSection load='2biw' size='340' side='right' caption='[[2biw]], [[Resolution|resolution]] 2.39&Aring;' scene=''>

<table><tr><td colspan='2'>[[2biw]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Aphanocapsa_sp._(strain_n-1) Aphanocapsa sp. (strain n-1)]. The June 2005 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Carotenoid Oxygenase'' by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2005_6 10.2210/rcsb_pdb/mom_2005_6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BIW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BIW FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3ON:(3R)-3-HYDROXY-8-APOCAROTENOL'>3ON</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bix|2bix]]</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2biw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2biw OCA], [http://pdbe.org/2biw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2biw RCSB], [http://www.ebi.ac.uk/pdbsum/2biw PDBsum]</span></td></tr>

[[http://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.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bi/2biw_consurf.spt"</scriptWhenChecked>

</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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== 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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 2biw" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Al-Babili, S]]

[[Category: Beyer, P]]

[[Category: Kloer, D P]]

[[Category: Ruch, S]]

[[Category: Schulz, G E]]

[[Category: Retinal formation]]