7oc6
From Proteopedia
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(New page: '''Unreleased structure''' The entry 7oc6 is ON HOLD Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Selenomethionine derivative of alpha-humulene synthase AsR6 from Sarocladium schorii== | |
| + | <StructureSection load='7oc6' size='340' side='right'caption='[[7oc6]], [[Resolution|resolution]] 2.01Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OC6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OC6 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]] 2.01Å</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=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7oc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oc6 OCA], [https://pdbe.org/7oc6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oc6 RCSB], [https://www.ebi.ac.uk/pdbsum/7oc6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oc6 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The non-canonical terpene cyclase AsR6 is responsible for the formation of 2E,6E,9E-humulene during the biosynthesis of the tropolone sesquiterpenoid (TS) xenovulene A. The structures of unliganded AsR6 and of AsR6 in complex with an in crystallo cyclized reaction product and thiolodiphosphate reveal a new farnesyl diphosphate binding motif that comprises a unique binuclear Mg2+cluster and an essential K289 residue that is conserved in all humulene synthases involved in TS formation. Structure-based sitedirected mutagenesis of AsR6 and its homologue EupR3 identify a single residue, L285/M261, that controls the production of either 2E,6E,9E- or 2Z,6E,9E-humulene. A possible mechanism for the observed stereoselectivity was investigated using different isoprenoid precursors and results demonstrate that M261 has gatekeeping control over product formation. | ||
| - | + | Understanding and Engineering the Stereoselectivity of Humulene Synthase.,Schotte C, Lukat P, Deuschmann A, Blankenfeldt W, Cox RJ Angew Chem Int Ed Engl. 2021 Jun 28. doi: 10.1002/anie.202106718. PMID:34180566<ref>PMID:34180566</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7oc6" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Blankenfeldt W]] | ||
| + | [[Category: Cox RJ]] | ||
| + | [[Category: Deuschmann A]] | ||
| + | [[Category: Lukat P]] | ||
| + | [[Category: Schotte C]] | ||
Current revision
Selenomethionine derivative of alpha-humulene synthase AsR6 from Sarocladium schorii
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