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  Vinorine synthase from Rauvolfia: the first example of crystallization and preliminary X-ray diffraction analysis of an enzyme of the BAHD superfamily

Ma, X., Koepke, J., Bayer, A., Linhard, V., Fritzsch, G., Zhang, B., et al. (2004). Vinorine synthase from Rauvolfia: the first example of crystallization and preliminary X-ray diffraction analysis of an enzyme of the BAHD superfamily. Biochimica et Biophysica Acta-Proteins and Proteomics, 1701(1-2), 129-132. doi:10.1016/j.bbapap.2004.06.011.

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 Creators:
Ma, Xueyan1, Author
Koepke, Jürgen2, Author              
Bayer, Anja1, Author
Linhard, Verena2, Author              
Fritzsch, Günter2, Author              
Zhang, Bin3, Author
Michel, Hartmut2, Author              
Stöckigt, Joachim1, Author
Affiliations:
1Department of Pharmaceutical Biology, Institute of Pharmacy, Johannes Gutenberg-University Mainz, Staudinger Weg 5, 55099 Mainz, Germany, ou_persistent22              
2Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
3Institute of Physical Chemistry, Johannes Gutenberg-University Mainz, Welderweg 11-15, 55099 Mainz, Germany, ou_persistent22              

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Free keywords: Acetyltransferase;Vinorine synthase; BAHD superfamily; Crystallization; Ajmaline biosynthesis
 Abstract: Crystals of vinorine synthase (VS) from medicinal plant Rauvolfia serpentina expressed in Escherichia coli have been obtained by the hanging-drop technique at 305 K with ammonium sulfate and PEG 400 as precipitants. The enzyme is involved in the biosynthesis of the antiarrhythmic drug ajmaline and is a member of the BAHD superfamily of acyltransferases. So far, no three-dimensional structure of a member of this enzyme family is known. The crystals belong to the space group P212121 with cell dimensions of a=82.3 A, b=89.6 A and c=136.2 A. Under cryoconditions (120 K), a complete data set up to 2.8 A was collected at a synchrotron source.

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Language(s): eng - English
 Dates: 2004-06-222004-05-052004-07-252004-09-01
 Publication Status: Published in print
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.bbapap.2004.06.011
PMID: 15450182
 Degree: -

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Title: Biochimica et Biophysica Acta-Proteins and Proteomics
  Other : BBA-Proteins Proteomics
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 1701 (1-2) Sequence Number: - Start / End Page: 129 - 132 Identifier: ISSN: 1570-9639
CoNE: https://pure.mpg.de/cone/journals/resource/954926938702_5