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

Ma, Xueyan; Koepke, Jürgen; Bayer, Anja; Linhard, Verena; Fritzsch, Günter; Zhang, Bin; Michel, Hartmut; Stöckigt, Joachim

doi:10.1016/j.bbapap.2004.06.011

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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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Datensatz-Permalink: https://hdl.handle.net/11858/00-001M-0000-0024-DAC7-D Versions-Permalink: https://hdl.handle.net/21.11116/0000-000B-A2EC-4

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Urheber:
Ma, Xueyan¹, Autor
Koepke, Jürgen², Autor
Bayer, Anja¹, Autor
Linhard, Verena², Autor
Fritzsch, Günter², Autor
Zhang, Bin³, Autor
Michel, Hartmut², Autor
Stöckigt, Joachim¹, Autor

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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Schlagwörter: Acetyltransferase;Vinorine synthase; BAHD superfamily; Crystallization; Ajmaline biosynthesis

Zusammenfassung: 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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Sprache(n): eng - English

Datum: Geändert: 2004-06-22Eingereicht: 2004-05-05Online veröffentlicht: 2004-07-25Erschienen: 2004-09-01

Publikationsstatus: Erschienen

Seiten: 4

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Art der Begutachtung: Expertenbegutachtung

Identifikatoren: DOI: 10.1016/j.bbapap.2004.06.011
PMID: 15450182

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Titel: Biochimica et Biophysica Acta-Proteins and Proteomics

Andere : BBA-Proteins Proteomics

Genre der Quelle: Zeitschrift

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Ort, Verlag, Ausgabe: Amsterdam : Elsevier

Seiten: - Band / Heft: 1701 (1-2) Artikelnummer: - Start- / Endseite: 129 - 132 Identifikator: ISSN: 1570-9639
CoNE: https://pure.mpg.de/cone/journals/resource/954926938702_5

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