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6b86
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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]] 2.20Å' scene=''> | + | <StructureSection load='6b86' size='340' side='right'caption='[[6b86]], [[Resolution|resolution]] 2.20Å' 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 [ | + | <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]] 2.2Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <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®/PubMed®, 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: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Neurospora crassa OR74A]] |
| - | [[Category: | + | [[Category: Hill HE]] |
| - | [[Category: | + | [[Category: Kiser PD]] |
| - | + | ||
Current revision
2.2A Crystal Structure of Co-CAO1
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