Membered ring (B), a pyrrole ring (C) along with a seven-membered ring
Membered ring (B), a pyrrole ring (C) along with a seven-membered ring (D). The five-membered rings A and E exhibit envelope conformations (C atoms as flaps) while ring C is planar. Ring B exhibits a twist-chair conformation because of fusion with pyrrole ring C when ring D adopts a chair conformation. The junction involving rings A and B is cis. Inside the crystal, weak C–H interactions involving the two carbonyl groups, a methylene plus 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 two.66 2.63 D 3.531 (4) 3.595 (three) three.496 (four) D–H 161 162Symmetry codes: (i) 1; y 1; ; (ii) x; y; z 1; (iii) x 1; y; z.Associated literatureFor general background to the structures and biological activity of stemona alkaloids, see: Pilli et al. (2010). For the antitussive activity of epibisdehydroneotuberostemonine J as well as other stemona alkaloids, see: Chung et al. (2003); Xu et al. (2010). For other properties of and studies 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).Data collection: Intelligent (Bruker, 1998); cell refinement: Clever and SAINT (Bruker, 1998); data reduction: SAINT and XPREP (Bruker, 1998); system(s) applied to solve structure: SHELXS97 (Sheldrick, 2008); plan(s) utilised to refine structure: SHELXL97 (Sheldrick, 2008); molecular graphics: XP in SHELXTL (Sheldrick, 2008); software utilised to prepare material for publication: SHELXTL.This work was supported by a grant on the Guangdong Higher Level Talent Scheme (RWJ) from Guangdong province as well as the Basic Research Funds for the Cental Universities (21612603) from the Ministry of Education, P. R. of China.Supplementary data and figures for this paper are available in the IUCr electronic archives (Reference: ZL2558).
NIH Public AccessRANTES/CCL5 Protein Biological Activity Author ManuscriptBiochemistry. Author manuscript; accessible in PMC 2014 April 30.Published in final edited type as: Biochemistry. 2013 April 30; 52(17): 2874887. doi:ten.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) working with a mechanism that involves organic radicals. The FGly residue plays a distinctive function as a cofactor inside a class of enzymes termed arylsulfatases, which catalyze the hydrolysis of several organosulfate monoesters. anSMEcpe has been shown to be a member of the GDF-11/BMP-11 Protein Accession radical Sadenosylmethionine (SAM) loved ones 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 in addition to the [4FeS] cluster harbored by all radical SAM (RS) enzymes,.