Membered ring (B), a pyrrole ring (C) plus a seven-membered ring
Membered ring (B), a pyrrole ring (C) and a seven-membered ring (D). The five-membered rings A and E exhibit envelope conformations (C atoms as flaps) even though ring C is planar. Ring B exhibits a twist-chair conformation resulting from fusion with pyrrole ring C though ring D adopts a chair conformation. The junction between rings A and B is cis. Within the crystal, weak C–H interactions involving the two carbonyl groups, a methylene and also 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 two.60 2.66 two.63 D 3.531 (4) three.595 (3) three.496 (4) D–H 161 162Symmetry codes: (i) 1; y 1; ; (ii) x; y; z 1; (iii) x 1; y; z.Associated literatureFor general background towards the structures and biological activity of stemona alkaloids, see: Pilli et al. (2010). For the antitussive activity of epibisdehydroneotuberostemonine J and also 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 related isomers, see: Pham et al. (2002).Information collection: Intelligent (Bruker, 1998); cell refinement: Clever and SAINT (Bruker, 1998); data reduction: SAINT and XPREP (Bruker, 1998); program(s) used to solve structure: SHELXS97 (Sheldrick, 2008); plan(s) made use of to refine structure: SHELXL97 (Sheldrick, 2008); molecular graphics: XP in SHELXTL (Sheldrick, 2008); software program used to prepare material for publication: SHELXTL.This work was supported by a grant with the Guangdong Higher Level Talent Scheme (RWJ) from Guangdong province and the Fundamental HSV-2 Species Investigation Funds for the Cental Universities (21612603) from the Ministry of Education, P. R. of China.Supplementary data and figures for this paper are obtainable from the IUCr electronic archives (Reference: ZL2558).
NIH Public AccessAuthor ManuscriptBiochemistry. Author manuscript; out there in PMC 2014 April 30.Published in final edited form as: Biochemistry. 2013 April 30; 52(17): 2874887. doi:10.1021bi400136u.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, USAAbstractThe anaerobic sulfatase maturating enzyme from Clostridium perfringens (anSMEcpe) catalyzes the two-electron oxidation of a cysteinyl residue on a cognate protein to a formyglycyl residue (FGly) using a mechanism that requires organic CDK11 Species radicals. The FGly residue plays a exceptional part as a cofactor inside a class of enzymes termed arylsulfatases, which catalyze the hydrolysis of several organosulfate monoesters. anSMEcpe has been shown to become a member of your 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 contains as well as the [4FeS] cluster harbored by all radical SAM (RS) enzymes,.