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Enroth, Cristofer
Publications (3 of 3) Show all publications
Enroth, C. & Strid, Å. (2008). Crystal structure of a protein, structurally related to glycosyltransferases, encoded in the Rhodobacter blasticus atp operon. Biochimica et Biophysica Acta - Proteins and Proteomics, 1784(2), 379-384
Open this publication in new window or tab >>Crystal structure of a protein, structurally related to glycosyltransferases, encoded in the Rhodobacter blasticus atp operon
2008 (English)In: Biochimica et Biophysica Acta - Proteins and Proteomics, ISSN 1570-9639, E-ISSN 1878-1454, Vol. 1784, no 2, p. 379-384Article in journal (Refereed) Published
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.

Place, publisher, year, edition, pages
Amsterdam: Elsevier/North Holland, 2008
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy) Medical and Health Sciences
Research subject
Biochemistry
Identifiers
urn:nbn:se:oru:diva-4153 (URN)10.1016/j.bbapap.2007.11.005 (DOI)
Available from: 2008-10-14 Created: 2008-10-14 Last updated: 2017-12-14Bibliographically approved
Hu, B., Collini, M., Unwalla, R., Miller, C., Singhaus, R., Quinet, E., . . . Wrobel, J. (2006). Discovery of phenyl acetic acid substituted quinolines as novel liver X receptor agonists for the treatment of atherosclerosis. Journal of Medicinal Chemistry, 49(21), 6151-6154
Open this publication in new window or tab >>Discovery of phenyl acetic acid substituted quinolines as novel liver X receptor agonists for the treatment of atherosclerosis
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2006 (English)In: Journal of Medicinal Chemistry, ISSN 0022-2623, E-ISSN 1520-4804, Vol. 49, no 21, p. 6151-6154Article in journal (Refereed) Published
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.

National Category
Pharmaceutical Sciences
Research subject
Biochemistry
Identifiers
urn:nbn:se:oru:diva-4127 (URN)10.1021/jm0609566 (DOI)17034119 (PubMedID)
Note
Letter.Available from: 2007-11-06 Created: 2007-11-06 Last updated: 2018-01-13Bibliographically approved
Scherbak, N., Brosché, M., Ala-Häivälä, A., Olsson, A., Enroth, C., Eriksson, L. A., . . . Strid, Å. Plant SAD proteins: characterization of the tetrameric Pisum sativum protein.
Open this publication in new window or tab >>Plant SAD proteins: characterization of the tetrameric Pisum sativum protein
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(English)Manuscript (preprint) (Other academic)
National Category
Biochemistry and Molecular Biology Biological Sciences
Research subject
Biochemistry; Biology
Identifiers
urn:nbn:se:oru:diva-2939 (URN)
Available from: 2005-11-11 Created: 2005-11-11 Last updated: 2017-10-18Bibliographically approved
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