View source for 6sbe


==Structure of type II terpene cyclase MstE_D109N from Scytonema in complex with geranylgeranyl dihydroxybenzoate (substrate)==
<StructureSection load='6sbe' size='340' side='right'caption='[[6sbe]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6sbe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Scytonema_sp._PCC_10023 Scytonema sp. PCC 10023]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SBE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SBE 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]] 1.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=L4E:geranylgeranyl+dihydroxybenzoate'>L4E</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=6sbe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sbe OCA], [https://pdbe.org/6sbe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sbe RCSB], [https://www.ebi.ac.uk/pdbsum/6sbe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sbe ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A2D1CM82_9CYAN A0A2D1CM82_9CYAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Class II terpene cyclases, such as oxidosqualene and squalene-hopene cyclases, catalyse some of the most complex polycyclization reactions. They minimally exhibit a beta,gamma-didomain architecture that has been evolutionarily repurposed in a wide range of terpene-processing enzymes and likely resulted from a fusion of unidentified monodomain proteins. Although single domain class I terpene cyclases have already been identified, the corresponding class II counterparts have not been previously reported. Here we present high-resolution X-ray structures of a monodomain class II cyclase, merosterolic acid synthase (MstE). With a minimalistic beta-domain architecture, this cyanobacterial enzyme is able to construct four rings in cytotoxic meroterpenoids with a sterol-like topology. The structures with bound substrate, product, and inhibitor provide detailed snapshots of a cyclization mechanism largely governed by residues located in a noncanonical enzyme region. Our results complement the few known class II cyclase crystal structures, while also indicating that archaic monodomain cyclases might have already catalyzed complex reaction cascades.

A monodomain class II terpene cyclase assembles complex isoprenoid scaffolds.,Moosmann P, Ecker F, Leopold-Messer S, Cahn JKB, Dieterich CL, Groll M, Piel J Nat Chem. 2020 Aug 10. pii: 10.1038/s41557-020-0515-3. doi:, 10.1038/s41557-020-0515-3. PMID:32778689<ref>PMID:32778689</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6sbe" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Scytonema sp. PCC 10023]]
[[Category: Cahn JKB]]
[[Category: Ecker F]]
[[Category: Groll M]]
[[Category: Leopold-Messer S]]
[[Category: Moosmann P]]
[[Category: Piel J]]