View source for 5lvw


==XiaF (FADH2) from Streptomyces sp.==
<StructureSection load='5lvw' size='340' side='right'caption='[[5lvw]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5lvw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LVW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LVW 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]] 2.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=IND:INDOLE'>IND</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=5lvw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lvw OCA], [https://pdbe.org/5lvw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lvw RCSB], [https://www.ebi.ac.uk/pdbsum/5lvw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lvw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/I7IIA9_9ACTN I7IIA9_9ACTN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Terpenoid natural products comprise a wide range of molecular architectures that typically result from C-C bond formations catalysed by classical type I/II terpene cyclases. However, the molecular diversity of biologically active terpenoids is substantially increased by fully unrelated, non-canonical terpenoid cyclases. Their evolutionary origin has remained enigmatic. Here we report the in vitro reconstitution of an unusual flavin-dependent bacterial indoloterpenoid cyclase, XiaF, together with a designated flavoenzyme-reductase (XiaP) that mediates a key step in xiamycin biosynthesis. The crystal structure of XiaF with bound FADH2 (at 2.4 A resolution) and phylogenetic analyses reveal that XiaF is, surprisingly, most closely related to xenobiotic-degrading enzymes. Biotransformation assays show that XiaF is a designated indole hydroxylase that can be used for the production of indigo and indirubin. We unveil a cryptic hydroxylation step that sets the basis for terpenoid cyclization and suggest that the cyclase has evolved from xenobiotics detoxification enzymes.

Cryptic indole hydroxylation by a non-canonical terpenoid cyclase parallels bacterial xenobiotic detoxification.,Kugel S, Baunach M, Baer P, Ishida-Ito M, Sundaram S, Xu Z, Groll M, Hertweck C Nat Commun. 2017 Jun 15;8:15804. doi: 10.1038/ncomms15804. PMID:28643772<ref>PMID:28643772</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5lvw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces sp]]
[[Category: Baer P]]
[[Category: Baunach M]]
[[Category: Groll M]]
[[Category: Hertweck C]]
[[Category: Ishida-Ito M]]
[[Category: Kugel S]]
[[Category: Sundaram S]]
[[Category: Xu Z]]