2biw: Difference between revisions

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 <StructureSection load='2biw' size='340' side='right'caption='[[2biw]], [[Resolution|resolution]] 2.39&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2biw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aphanocapsa_sp._(strain_n-1) Aphanocapsa sp. (strain n-1)]. The June 2005 RCSB PDB [https://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 [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2BIW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2biw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. The June 2005 RCSB PDB [https://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 [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2BIW FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3ON:(3R)-3-HYDROXY-8-APOCAROTENOL'>3ON</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.39&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2bix|2bix]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3ON:(3R)-3-HYDROXY-8-APOCAROTENOL'>3ON</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2biw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2biw OCA], [https://pdbe.org/2biw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2biw RCSB], [https://www.ebi.ac.uk/pdbsum/2biw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2biw ProSAT]</span></td></tr>
 </table>
 == 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.
+[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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
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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/main_output.php?pdb_ID=2biw 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.
-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>
-</div>
-<div class="pdbe-citations 2biw" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
@@ Line 36: / Line 25: @@
 [[Category: Large Structures]]
 [[Category: RCSB PDB Molecule of the Month]]
-[[Category: Al-Babili, S]]
+[[Category: Synechocystis sp. PCC 6803]]
-[[Category: Beyer, P]]
+[[Category: Al-Babili S]]
-[[Category: Kloer, D P]]
+[[Category: Beyer P]]
-[[Category: Ruch, S]]
+[[Category: Kloer DP]]
-[[Category: Schulz, G E]]
+[[Category: Ruch S]]
-[[Category: Carotenoid cleavage]]
+[[Category: Schulz GE]]
-[[Category: Dioxygenase]]
-[[Category: Non-heme iron]]
-[[Category: Oxidoreductase]]
-[[Category: Oxygenase]]
-[[Category: Retinal formation]]