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5u97
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Co-CAO1 in complex with piceatannol== | |
| + | <StructureSection load='5u97' size='340' side='right'caption='[[5u97]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5u97]] 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=5U97 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5U97 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEZ:BENZOIC+ACID'>BEZ</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=PIT:PICEATANNOL'>PIT</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=5u97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5u97 OCA], [https://pdbe.org/5u97 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5u97 RCSB], [https://www.ebi.ac.uk/pdbsum/5u97 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5u97 ProSAT]</span></td></tr> | ||
| + | </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 (CCOs) are non-heme iron enzymes that catalyze scission of alkene groups in carotenoids and stilbenoids to form biologically important products. CCOs possess a rare four-His iron center whose resting-state structure and interaction with substrates are incompletely understood. Here, we address this knowledge gap through a comprehensive structural and spectroscopic study of three phyletically diverse CCOs. The crystal structure of a fungal stilbenoid-cleaving CCO, CAO1, reveals strong similarity between its iron center and those of carotenoid-cleaving CCOs, but with a markedly different substrate-binding cleft. These enzymes all possess a five-coordinate high-spin Fe(II) center with resting-state Fe-His bond lengths of approximately 2.15 A. This ligand set generates an iron environment more electropositive than those of other non-heme iron dioxygenases as observed by Mossbauer isomer shifts. Dioxygen (O2) does not coordinate iron in the absence of substrate. Substrates bind away ( approximately 4.7 A) from the iron and have little impact on its electronic structure, thus excluding coordination-triggered O2 binding. However, substrate binding does perturb the spectral properties of CCO Fe-NO derivatives, indicating proximate organic substrate and O2-binding sites, which might influence Fe-O2 interactions. Together, these data provide a robust description of the CCO iron center and its interactions with substrates and substrate mimetics that illuminates commonalities as well as subtle and profound structural differences within the CCO family. | ||
| - | + | Structure and Spectroscopy of Alkene-Cleaving Dioxygenases Containing an Atypically Coordinated Non-Heme Iron Center.,Sui X, Weitz AC, Farquhar ER, Badiee M, Banerjee S, von Lintig J, Tochtrop GP, Palczewski K, Hendrich MP, Kiser PD Biochemistry. 2017 Jun 6;56(22):2836-2852. doi: 10.1021/acs.biochem.7b00251. Epub, 2017 May 19. PMID:28493664<ref>PMID:28493664</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5u97" style="background-color:#fffaf0;"></div> |
| - | [[Category: Banerjee | + | == References == |
| - | [[Category: Kiser | + | <references/> |
| - | [[Category: Palczewski | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Neurospora crassa OR74A]] | ||
| + | [[Category: Banerjee S]] | ||
| + | [[Category: Kiser PD]] | ||
| + | [[Category: Palczewski K]] | ||
| + | [[Category: Sui X]] | ||
Current revision
Crystal structure of Co-CAO1 in complex with piceatannol
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