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  • 1.
    Enroth, Cristofer
    et al.
    Örebro University, Department of Natural Sciences.
    Strid, Åke
    Örebro University, Department of Natural Sciences.
    Crystal structure of a protein, structurally related to glycosyltransferases, encoded in the Rhodobacter blasticus atp operon2008In: Biochimica et Biophysica Acta - Proteins and Proteomics, ISSN 1570-9639, E-ISSN 1878-1454, Vol. 1784, no 2, p. 379-384Article in journal (Refereed)
    Abstract [en]

    The F1-ATP synthase atp operon in the proteobacterium Rhodobacter blasticus contains six open reading frames, encoding six hypothetical proteins. Five of these subunits, in the stoichiometry (ab)3gde make up the catalytic F1-ATP synthase complex similarly in bacteria, chloroplasts and mitochondria. The sixth gene of the Rb. blasticus atp operon, urf6, shows very little sequence homology to any protein of known structure or function. The gene has previously been cloned, the product (called majastridin) has been heterologously expressed in Escherichia coli, and purified to high homogeneity (Brosché et al. (1998) Eur. J. Biochem. 255: 87-92). We have solved the X-ray crystal structure and refined a model of majastridin to atomic resolution. Here we present the crystal structures of apo-majastridin and the complex of majastridin with Mn2+ and UDP and show it has extensive structural similarity to glycosyltransferases (EC 2.4). This is the first structure determined from a new group of distantly related bacterial proteins of at least six members. They share the identical amino acids that bind Mn2+and a triplet of amino acids in the putative sugar-binding site.

  • 2. Hu, Baihua
    et al.
    Collini, Michael
    Unwalla, Rayomand
    Miller, Christopher
    Singhaus, Robert
    Quinet, Elaine
    Savio, Dawn
    Halpern, Anita
    Basso, Michael
    Keith, James
    Clerin, Valerie
    Chen, Liang
    Resmini, Christine
    Liu, Qiang-Yuan
    Feingold, Irene
    Huselton, Christine
    Azam, Farooq
    Farnegardh, Mathias
    Enroth, Cristofer
    Örebro University, Department of Natural Sciences.
    Bonn, Tomas
    Goos-Nilsson, Annika
    Wilhelmsson, Anna
    Nambi, Ponnal
    Wrobel, Jay
    Discovery of phenyl acetic acid substituted quinolines as novel liver X receptor agonists for the treatment of atherosclerosis2006In: Journal of Medicinal Chemistry, ISSN 0022-2623, E-ISSN 1520-4804, Vol. 49, no 21, p. 6151-6154Article in journal (Refereed)
    Abstract [en]

    A structure-based approach was used to optimize our new class of quinoline LXR modulators leading to phenyl acetic acid substituted quinolines 15 and 16. Both compounds displayed good binding affinity for LXRâ and LXRR and were potent activators in LBD transactivation assays. The compounds also increased expression of ABCA1 and stimulated cholesterol efflux in THP-1 cells. Quinoline 16 showed good oral bioavailability and in vivo efficacy in a LDLr knockout mouse model for lesions.

  • 3.
    Scherbak, Nikolai
    et al.
    Örebro University, Department of Natural Sciences.
    Brosché, Mikael
    Ala-Häivälä, Anneli
    Olsson, Annika
    Enroth, Cristofer
    Örebro University, Department of Natural Sciences.
    Eriksson, Leif A.
    Örebro University, Department of Natural Sciences.
    Nilsson, Fredrik
    Strid, Åke
    Örebro University, Department of Natural Sciences.
    Plant SAD proteins: characterization of the tetrameric Pisum sativum proteinManuscript (preprint) (Other academic)
1 - 3 of 3
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