View source for 5u97


==Crystal structure of Co-CAO1 in complex with piceatannol==
<StructureSection load='5u97' size='340' side='right'caption='[[5u97]], [[Resolution|resolution]] 1.85&Aring;' 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]] 1.85&#8491;</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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5u97" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Neurospora crassa OR74A]]
[[Category: Banerjee S]]
[[Category: Kiser PD]]
[[Category: Palczewski K]]
[[Category: Sui X]]