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==Selinadiene Synthase apo and in complex with diphosphate==
==Selinadiene Synthase apo and in complex with diphosphate==
<StructureSection load='4okm' size='340' side='right' caption='[[4okm]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='4okm' size='340' side='right'caption='[[4okm]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4okm]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OKM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OKM FirstGlance]. <br>
<table><tr><td colspan='2'>[[4okm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_pristinaespiralis_ATCC_25486 Streptomyces pristinaespiralis ATCC 25486]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OKM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OKM FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PPV:PYROPHOSPHATE'>PPV</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4okz|4okz]], [[1ps1|1ps1]], [[4mc0|4mc0]], [[4mc3|4mc3]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PPV:PYROPHOSPHATE'>PPV</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Squalene_synthase Squalene synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.21 2.5.1.21] </span></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=4okm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4okm OCA], [https://pdbe.org/4okm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4okm RCSB], [https://www.ebi.ac.uk/pdbsum/4okm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4okm ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4okm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4okm OCA], [http://pdbe.org/4okm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4okm RCSB], [http://www.ebi.ac.uk/pdbsum/4okm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4okm ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/SEDS_STRE2 SEDS_STRE2] Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) to yield the bicyclic sesquiterpene selina-4(15),7(11)-diene via a 1,10-cyclization, which requires the abstraction of the pyrophosphate from FPP leading to a (E,E)-germacradienyl cation (PubMed:23307484, PubMed:24890698). The only accepted substrate is (2E,6E)-farnesyl diphosphate (FPP) (PubMed:23307484, PubMed:24890698).<ref>PMID:23307484</ref> <ref>PMID:24890698</ref>  
We present crystallographic and functional data of selina-4(15),7(11)-diene synthase (SdS) from Streptomyces pristinaespiralis in its open and closed (ligand-bound) conformation. We could identify an induced-fit mechanism by elucidating a rearrangement of the G1/2 helix-break motif upon substrate binding. This rearrangement highlights a novel effector triad comprising the pyrophosphate sensor Arg178, the linker Asp181, and the effector Gly182-O. This structural motif is strictly conserved in class I terpene cyclases from bacteria, fungi, and plants, including epi-isozizaene synthase (3KB9), aristolochene synthase (4KUX), bornyl diphosphate synthase (1N20), limonene synthase (2ONG), 5-epi-aristolochene synthase (5EAT), and taxa-4(5),11(12)-diene synthase (3P5R). An elaborate structure-based mutagenesis in combination with analysis of the distinct product spectra confirmed the mechanistic models of carbocation formation and stabilization in SdS.
 
Induced-Fit Mechanism in Class I Terpene Cyclases.,Baer P, Rabe P, Fischer K, Citron CA, Klapschinski TA, Groll M, Dickschat JS Angew Chem Int Ed Engl. 2014 May 30. doi: 10.1002/anie.201403648. PMID:24890698<ref>PMID:24890698</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4okm" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Squalene synthase]]
[[Category: Large Structures]]
[[Category: Baer, P]]
[[Category: Streptomyces pristinaespiralis ATCC 25486]]
[[Category: Citron, C A]]
[[Category: Baer P]]
[[Category: Dickschat, J S]]
[[Category: Citron CA]]
[[Category: Fischer, K]]
[[Category: Dickschat JS]]
[[Category: Groll, M]]
[[Category: Fischer K]]
[[Category: Klapschinski, T]]
[[Category: Groll M]]
[[Category: Rabe, P]]
[[Category: Klapschinski T]]
[[Category: Cyclase]]
[[Category: Rabe P]]
[[Category: Induced fit]]
[[Category: Open and closed conformation]]
[[Category: Pyrophosphate sensor]]
[[Category: Sesquiterpene]]
[[Category: Terpenoid]]
[[Category: Transferase]]
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