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| | ==Crystal structure of cobalt-substituted Synechocystis ACO== | | ==Crystal structure of cobalt-substituted Synechocystis ACO== |
| - | <StructureSection load='6big' size='340' side='right' caption='[[6big]], [[Resolution|resolution]] 2.21Å' scene=''> | + | <StructureSection load='6big' size='340' side='right'caption='[[6big]], [[Resolution|resolution]] 2.21Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6big]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Syny3 Syny3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BIG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BIG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6big]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803_substr._Kazusa Synechocystis sp. PCC 6803 substr. Kazusa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BIG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BIG FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</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]] 2.21Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6b86|6b86]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sll1541 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1111708 SYNY3])</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=6big FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6big OCA], [https://pdbe.org/6big PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6big RCSB], [https://www.ebi.ac.uk/pdbsum/6big PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6big ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/All-trans-8'-apo-beta-carotenal_15,15'-oxygenase All-trans-8'-apo-beta-carotenal 15,15'-oxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.75 1.13.11.75] </span></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=6big FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6big OCA], [http://pdbe.org/6big PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6big RCSB], [http://www.ebi.ac.uk/pdbsum/6big PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6big ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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. | + | [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. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: All-trans-8'-apo-beta-carotenal 15,15'-oxygenase]] | + | [[Category: Large Structures]] |
| - | [[Category: Syny3]] | + | [[Category: Synechocystis sp. PCC 6803 substr. Kazusa]] |
| - | [[Category: Kiser, P D]] | + | [[Category: Kiser PD]] |
| - | [[Category: Shi, W]] | + | [[Category: Shi W]] |
| - | [[Category: Sui, X]] | + | [[Category: Sui X]] |
| - | [[Category: Beta propeller]]
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| - | [[Category: Cobalt]]
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| - | [[Category: Dioxygenase]]
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| - | [[Category: Non-heme iron]]
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| - | [[Category: Oxidoreductase]]
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| Structural highlights
Function
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.
Publication Abstract from PubMed
Carotenoid cleavage oxygenases (CCO) are non-heme iron enzymes that catalyze oxidative cleavage of alkene bonds in carotenoid and stilbenoid substrates. Previously, we showed that the iron cofactor of CAO1, a resveratrol-cleaving member of this family, can be substituted with cobalt to yield a catalytically inert enzyme useful for trapping active site-bound stilbenoid substrates for structural characterization. Metal substitution may provide a general method for identifying the natural substrates for CCOs in addition to facilitating structural and biophysical characterization of CCO-carotenoid complexes under normal aerobic conditions. Here, we demonstrate the general applicability of cobalt substitution in a prototypical carotenoid cleaving CCO, apocarotenoid oxygenase (ACO) from Synechocystis. Among the non-native divalent metals investigated, cobalt was uniquely able to stably occupy the ACO metal binding site and inhibit catalysis. Analysis by X-ray crystallography and X-ray absorption spectroscopy demonstrate that the Co(II) forms of both ACO and CAO1 exhibit a close structural correspondence to the native Fe(II) enzyme forms. Hence, cobalt substitution is an effective strategy for generating catalytically inert but structurally intact forms of CCOs.
Preparation and characterization of metal-substituted carotenoid cleavage oxygenases.,Sui X, Farquhar ER, Hill HE, von Lintig J, Shi W, Kiser PD J Biol Inorg Chem. 2018 Aug;23(6):887-901. doi: 10.1007/s00775-018-1586-0. Epub, 2018 Jun 26. PMID:29946976[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sui X, Farquhar ER, Hill HE, von Lintig J, Shi W, Kiser PD. Preparation and characterization of metal-substituted carotenoid cleavage oxygenases. J Biol Inorg Chem. 2018 Aug;23(6):887-901. doi: 10.1007/s00775-018-1586-0. Epub, 2018 Jun 26. PMID:29946976 doi:http://dx.doi.org/10.1007/s00775-018-1586-0
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