View source for 7vtb


==Partially closed conformation of talaropentaene synthase cyclase domain==
<StructureSection load='7vtb' size='340' side='right'caption='[[7vtb]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7vtb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Talaromyces_verruculosus Talaromyces verruculosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VTB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VTB 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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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=7vtb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vtb OCA], [https://pdbe.org/7vtb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vtb RCSB], [https://www.ebi.ac.uk/pdbsum/7vtb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vtb ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
All known triterpenes are generated by triterpene synthases (TrTSs) from squalene or oxidosqualene(1). This approach is fundamentally different from the biosynthesis of short-chain (C10-C25) terpenes that are formed from polyisoprenyl diphosphates(2-4). In this study, two fungal chimeric class I TrTSs, Talaromyces verruculosus talaropentaene synthase (TvTS) and Macrophomina phaseolina macrophomene synthase (MpMS), were characterized. Both enzymes use dimethylallyl diphosphate and isopentenyl diphosphate or hexaprenyl diphosphate as substrates, representing the first examples, to our knowledge, of non-squalene-dependent triterpene biosynthesis. The cyclization mechanisms of TvTS and MpMS and the absolute configurations of their products were investigated in isotopic labelling experiments. Structural analyses of the terpene cyclase domain of TvTS and full-length MpMS provide detailed insights into their catalytic mechanisms. An AlphaFold2-based screening platform was developed to mine a third TrTS, Colletotrichum gloeosporioides colleterpenol synthase (CgCS). Our findings identify a new enzymatic mechanism for the biosynthesis of triterpenes and enhance understanding of terpene biosynthesis in nature.

Discovery of non-squalene triterpenes.,Tao H, Lauterbach L, Bian G, Chen R, Hou A, Mori T, Cheng S, Hu B, Lu L, Mu X, Li M, Adachi N, Kawasaki M, Moriya T, Senda T, Wang X, Deng Z, Abe I, Dickschat JS, Liu T Nature. 2022 Jun;606(7913):414-419. doi: 10.1038/s41586-022-04773-3. Epub 2022, Jun 1. PMID:35650436<ref>PMID:35650436</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7vtb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Talaromyces verruculosus]]
[[Category: Abe I]]
[[Category: Hui T]]
[[Category: Mori T]]