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==2.2A Crystal Structure of Co-CAO1==
==2.2A Crystal Structure of Co-CAO1==
<StructureSection load='6b86' size='340' side='right' caption='[[6b86]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='6b86' size='340' side='right'caption='[[6b86]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6b86]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B86 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6B86 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6b86]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Neurospora_crassa_OR74A Neurospora crassa OR74A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B86 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6B86 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 2.2&#8491;</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=6b86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b86 OCA], [http://pdbe.org/6b86 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6b86 RCSB], [http://www.ebi.ac.uk/pdbsum/6b86 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6b86 ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</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=6b86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b86 OCA], [https://pdbe.org/6b86 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6b86 RCSB], [https://www.ebi.ac.uk/pdbsum/6b86 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6b86 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CAO1_NEUCR CAO1_NEUCR] Dioxygenase that cleaves the interphenyl C-alpha-C-beta double bond of resveratrol to yield 3,5-dihydroxybenzaldehyde and 4-hydroxybenzaldehyde (PubMed:23893079, PubMed:28493664). Cleaves also piceatannol, a compound that differs from resveratrol only in the occurrence of an additional hydroxyl group, which leads to the production of 3,4-dihydroxybenzaldehyde and 3,5-hydroxybenzaldehyde (PubMed:23893079 PubMed:28493664). Is not able to cleave trans-stilbene, 4-monohydroxy-trans-stilbene, 3,5-dihydroxy-trans-stilbene (pinosylvin), trismethoxy-resveratrol, and 3,3',5-trihydroxy-4'-methoxystilbene-3-O-beta-D-glucoside (PubMed:23893079). Is not involved in carotenoid metabolism (PubMed:23893079).<ref>PMID:23893079</ref> <ref>PMID:28493664</ref>
<div style="background-color:#fffaf0;">
== 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<ref>PMID:29946976</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6b86" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Hill, H E]]
[[Category: Large Structures]]
[[Category: Kiser, P D]]
[[Category: Neurospora crassa OR74A]]
[[Category: Beta-propeller]]
[[Category: Hill HE]]
[[Category: Dioxygenase]]
[[Category: Kiser PD]]
[[Category: Oxidoreductase]]
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