7etk

The complex structure of FtmOx1 bond with fumitremorgen B at 1.22 angstrom

spinqualitylabelsall models 7etk, resolution 1.22Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7etk is a 2 chain structure with sequence from Aspergillus fumigatus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.2202743Å Ligands: 4Q1, AKG, EDO, FE2, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FTMF_ASPFU Catalyzes the conversion of fumitremorgin B to verruculogen. Publication Abstract from PubMed The 2-oxoglutarate (2OG)-dependent non-heme FtmOx1 catalyzes the endoperoxide biosynthesis of verruculogen. Although several mechanistic studies have been carried out, the catalytic mechanism of FtmOx1 is not well determined due to the lack of the reliable complex structure of FtmOx1 with fumitremorgin B. Here we provided the X-ray structure of the ternary complex FtmOx1*2OG*fumitremorgin B at resolution of 1.22 A. Our structures show that the binding of fumitremorgin B has induced the significant compression of the active pocket and Y68 in close proximity to C26 of the substrate. Further MD simulation and QM/MM calculations support the CarC-like mechanism proposed by Bollinger and coworkers, in which Y68 rather than Y224 acts as the H atom donor for quenching the C26-centered substrate radical. Our work is consistent with all available experimental data and highlights the importance of the accurate complex structure in mechanistic study of enzymatic catalysis. Structural Insight into the Catalytic Mechanism of the Endoperoxide Synthase FtmOx1.,Zhou J, Wu L, Wang Z, Cen Y, Wang B Angew Chem Int Ed Engl. 2021 Nov 18. doi: 10.1002/anie.202112063. PMID:34796596 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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