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| <StructureSection load='5guk' size='340' side='right'caption='[[5guk]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='5guk' size='340' side='right'caption='[[5guk]], [[Resolution|resolution]] 2.00Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[5guk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Strc1 Strc1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GUK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GUK FirstGlance]. <br> | | <table><tr><td colspan='2'>[[5guk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._CL190 Streptomyces sp. CL190]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GUK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GUK FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 2Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5gul|5gul]]</td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=5guk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5guk OCA], [http://pdbe.org/5guk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5guk RCSB], [http://www.ebi.ac.uk/pdbsum/5guk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5guk ProSAT]</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=5guk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5guk OCA], [https://pdbe.org/5guk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5guk RCSB], [https://www.ebi.ac.uk/pdbsum/5guk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5guk ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/X5IYJ5_STRC1 X5IYJ5_STRC1] |
| We report the three-dimensional structure of cyclolavandulyl diphosphate (CLPP) synthase (CLDS), which consecutively catalyzes the condensation of two molecules of dimethylallyl diphosphate (DMAPP) followed by cyclization to form a cyclic monoterpene, CLPP. The structures of apo-CLDS and CLDS in complex with Tris, pyrophosphate, and Mg(2+) ion were refined at 2.00 A resolution and 1.73 A resolution, respectively. CLDS adopts a typical fold for cis-prenyl synthases and forms a homo-dimeric structure. An in vitro reaction using a regiospecifically (2) H-substituted DMAPP substrate revealed the intramolecular proton transfer mechanism of the CLDS reaction. The CLDS structure and structure-based mutagenesis provide mechanistic insights into this unprecedented terpene synthase. The combination of structural and mechanistic insights advances the knowledge of intricate terpene synthase-catalyzed reactions.
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| Structure and Mechanism of the Monoterpene Cyclolavandulyl Diphosphate Synthase that Catalyzes Consecutive Condensation and Cyclization.,Tomita T, Kobayashi M, Karita Y, Yasuno Y, Shinada T, Nishiyama M, Kuzuyama T Angew Chem Int Ed Engl. 2017 Nov 20;56(47):14913-14917. doi:, 10.1002/anie.201708474. Epub 2017 Oct 11. PMID:28922556<ref>PMID:28922556</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 5guk" style="background-color:#fffaf0;"></div>
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| == References ==
| |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Strc1]] | | [[Category: Streptomyces sp. CL190]] |
| [[Category: Kobayashi, M]] | | [[Category: Kobayashi M]] |
| [[Category: Kuzuyama, T]] | | [[Category: Kuzuyama T]] |
| [[Category: Nishiyama, M]] | | [[Category: Nishiyama M]] |
| [[Category: Tomita, T]] | | [[Category: Tomita T]] |
| [[Category: Apo form]]
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| [[Category: Biosynthetic protein]]
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| [[Category: Cis-prenyltransferase]]
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| [[Category: Cyclolavandulyl diphosphate synthase]]
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| [[Category: Streptomyces sp. cl190]]
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