Five-membered rings A and E exhibit envelope conformations (C atoms as flaps) although ring C is planar. Ring B exhibits a twist-chair conformation resulting from fusion with pyrrole ring C even though ring D adopts a chair conformation. The junction among rings A and B is cis. In the crystal, weak C–H interactions involving the two carbonyl groups, a methylene along with a methyl group give rise to a three-dimensional network.TableHydrogen-bond geometry (A, ).D–H C5–H5A 2i C5–H5B 4ii C22–H22B 4iii D–H 0.97 0.97 0.96 H 2.60 2.66 2.63 D three.531 (four) three.595 (three) three.496 (four) D–H 161 162Symmetry codes: (i) 1; y 1; ; (ii) x; y; z 1; (iii) x 1; y; z.Related literatureFor general background to the structures and biological activity of stemona alkaloids, see: Pilli et al. (2010). For the antitussive activity of epibisdehydroneotuberostemonine J and other stemona alkaloids, see: Chung et al. (2003); Xu et al. (2010). For other properties of and research on Stemona alkaloids, see: Chung et al. (2003); Frankowski et al. (2008, 2011); Jiang et al. (2006); Zhang et al. (2011). For an absolute structure reference, see: Jiang et al. (2010). For connected isomers, see: Pham et al. (2002).Information collection: Wise (Bruker, 1998); cell refinement: Smart and SAINT (Bruker, 1998); data reduction: SAINT and XPREP (Bruker, 1998); plan(s) used to solve structure: SHELXS97 (Sheldrick, 2008); plan(s) utilised to refine structure: SHELXL97 (Sheldrick, 2008); molecular graphics: XP in SHELXTL (Sheldrick, 2008); software utilized to prepare material for publication: SHELXTL.This work was supported by a grant with the Guangdong High Level Talent Scheme (RWJ) from Guangdong province along with the Basic Research Funds for the Cental Universities (21612603) in the Ministry of Education, P. R. of China.Supplementary data and figures for this paper are out there from the IUCr electronic archives (Reference: ZL2558).
NIH Public AccessAuthor ManuscriptBiochemistry. Author manuscript; offered in PMC 2014 April 30.Published in final edited form as: Biochemistry. 2013 April 30; 52(17): 2874887. doi:10.1021/bi400136u.NIH-PA Author Manuscript NIH-PA Author Manuscript NIH-PA Author ManuscriptFurther Characterization of Cys-Type and Ser-Type Anaerobic Sulfatase Maturating Enzymes Suggests a Commonality in Mechanism of CatalysisTyler L. Grove, Jessica H. Ahlum, Rosie M. Qin Nicholas D. Lanz Matthew I. Radle, Carsten Krebs,, and Squire J. Booker,,Department of Chemistry, Pennsylvania State University, University Park, Pennsylvania 16802, USA�Departmentof Biochemistry and Molecular Biology, Pennsylvania State University, University Park, Pennsylvania 16802, D4 Receptor Antagonist Molecular Weight USAAbstractThe anaerobic sulfatase maturating enzyme from Clostridium perfringens (anSMEcpe) catalyzes the two-electron oxidation of a CXCR2 Antagonist Accession cysteinyl residue on a cognate protein to a formyglycyl residue (FGly) making use of a mechanism that entails organic radicals. The FGly residue plays a one of a kind role as a cofactor within a class of enzymes termed arylsulfatases, which catalyze the hydrolysis of a variety of organosulfate monoesters. anSMEcpe has been shown to become a member with the radical Sadenosylmethionine (SAM) family of enzymes, [4FeS] cluster equiring proteins that use a 5’deoxyadenosyl 5′-radical (5′-dA generated from a reductive cleavage of SAM to initiate radicalbased catalysis. Herein, we show that anSMEcpe consists of as well as the [4FeS] cluster harbored by all radical SAM (RS) enzymes, two further [4FeS] clusters, equivalent to the radical SAM protein AtsB.
