View source for 8rqh


==Crystal Structure of the flavoprotein monooxygenase TrlE from Streptomyces cyaneofuscatus Soc7==
<StructureSection load='8rqh' size='340' side='right'caption='[[8rqh]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8rqh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_cyaneofuscatus Streptomyces cyaneofuscatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8RQH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8RQH 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]] 2.5&#8491;</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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=8rqh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8rqh OCA], [https://pdbe.org/8rqh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8rqh RCSB], [https://www.ebi.ac.uk/pdbsum/8rqh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8rqh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A2S1JZI9_9ACTN A0A2S1JZI9_9ACTN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The non-benzenoid aromatic tropone ring is a structural motif of numerous microbial and plant natural products with potent bioactivities. In bacteria, tropone biosynthesis involves early steps of the widespread CoA-dependent phenylacetic acid (paa) catabolon, from which a shunt product is sequestered and surprisingly further utilized as a universal precursor for structurally and functionally diverse tropone derivatives such as tropodithietic acid or (hydroxy)tropolones. Here, we elucidate the biosynthesis of the antibiotic 3,7-dihydroxytropolone in Actinobacteria by in vitro pathway reconstitution using paa catabolic enzymes as well as dedicated downstream tailoring enzymes, including a thioesterase (TrlF) and two flavoprotein monooxygenases (TrlCD and TrlE). We furthermore mechanistically and structurally characterize the multifunctional key enzyme TrlE, which mediates an unanticipated ipso-substitution involving a hydroxylation and subsequent decarboxylation of the CoA-freed side chain, followed by ring oxidation to afford tropolone. This study showcases a remarkably efficient strategy for 3,7-dihydroxytropolone biosynthesis and illuminates the functions of the involved biosynthetic enzymes.

Biosynthesis of the bacterial antibiotic 3,7-dihydroxytropolone through enzymatic salvaging of catabolic shunt products.,Hoing L, Sowa ST, Toplak M, Reinhardt JK, Jakob R, Maier T, Lill MA, Teufel R Chem Sci. 2024 Apr 24;15(20):7749-7756. doi: 10.1039/d4sc01715c. eCollection 2024 , May 22. PMID:38784727<ref>PMID:38784727</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8rqh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces cyaneofuscatus]]
[[Category: Hoeing LS]]
[[Category: Jakob RP]]
[[Category: Maier T]]
[[Category: Sowa ST]]
[[Category: Teufel R]]