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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> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/X5IYJ5_STRC1 X5IYJ5_STRC1] |
| | <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: 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]]
| + | |
| - | [[Category: Biosynthetic protein]]
| + | |
| - | [[Category: Cis-prenyltransferase]]
| + | |
| - | [[Category: Cyclolavandulyl diphosphate synthase]]
| + | |
| - | [[Category: Streptomyces sp. cl190]]
| + | |
| Structural highlights
Function
X5IYJ5_STRC1
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tomita T, Kobayashi M, Karita Y, Yasuno Y, Shinada T, Nishiyama M, Kuzuyama T. Structure and Mechanism of the Monoterpene Cyclolavandulyl Diphosphate Synthase that Catalyzes Consecutive Condensation and Cyclization. Angew Chem Int Ed Engl. 2017 Nov 20;56(47):14913-14917. doi:, 10.1002/anie.201708474. Epub 2017 Oct 11. PMID:28922556 doi:http://dx.doi.org/10.1002/anie.201708474
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