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| | <StructureSection load='4okm' size='340' side='right'caption='[[4okm]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='4okm' size='340' side='right'caption='[[4okm]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4okm]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Stre2 Stre2]. 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='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='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='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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SSDG_02809, ZP_06911744 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=457429 STRE2])</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'>[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> |
| | + | == Function == |
| | + | [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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Squalene synthase]] | + | [[Category: Streptomyces pristinaespiralis ATCC 25486]] |
| - | [[Category: Stre2]]
| + | [[Category: Baer P]] |
| - | [[Category: Baer, P]] | + | [[Category: Citron CA]] |
| - | [[Category: Citron, C A]] | + | [[Category: Dickschat JS]] |
| - | [[Category: Dickschat, J S]] | + | [[Category: Fischer K]] |
| - | [[Category: Fischer, K]] | + | [[Category: Groll M]] |
| - | [[Category: Groll, M]] | + | [[Category: Klapschinski T]] |
| - | [[Category: Klapschinski, T]] | + | [[Category: Rabe P]] |
| - | [[Category: Rabe, P]] | + | |
| - | [[Category: Cyclase]]
| + | |
| - | [[Category: Induced fit]]
| + | |
| - | [[Category: Open and closed conformation]]
| + | |
| - | [[Category: Pyrophosphate sensor]]
| + | |
| - | [[Category: Sesquiterpene]]
| + | |
| - | [[Category: Terpenoid]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
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).[1] [2]
Publication Abstract from PubMed
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rabe P, Dickschat JS. Rapid chemical characterization of bacterial terpene synthases. Angew Chem Int Ed Engl. 2013 Feb 4;52(6):1810-2. doi: 10.1002/anie.201209103. , Epub 2013 Jan 10. PMID:23307484 doi:http://dx.doi.org/10.1002/anie.201209103
- ↑ Baer P, Rabe P, Fischer K, Citron CA, Klapschinski TA, Groll M, Dickschat JS. Induced-Fit Mechanism in Class I Terpene Cyclases. Angew Chem Int Ed Engl. 2014 May 30. doi: 10.1002/anie.201403648. PMID:24890698 doi:http://dx.doi.org/10.1002/anie.201403648
- ↑ Baer P, Rabe P, Fischer K, Citron CA, Klapschinski TA, Groll M, Dickschat JS. Induced-Fit Mechanism in Class I Terpene Cyclases. Angew Chem Int Ed Engl. 2014 May 30. doi: 10.1002/anie.201403648. PMID:24890698 doi:http://dx.doi.org/10.1002/anie.201403648
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