7oc6

Selenomethionine derivative of alpha-humulene synthase AsR6 from Sarocladium schorii

spinqualitylabelsall models 7oc6, resolution 2.01Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.01Å Ligands: GOL, MSE, SO4, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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