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  Crystal Structure of Vinorine Synthase, the First Representative of the BAHD Superfamily

Ma, X., Koepke, J., Panjikar, S., Fritzsch, G., & Stöckigt, J. (2005). Crystal Structure of Vinorine Synthase, the First Representative of the BAHD Superfamily. The Journal of Biological Chemistry, 280(14), 13576-13583. doi:10.1074/jbc.M414508200.

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 Creators:
Ma, Xueyan1, Author
Koepke, Jürgen2, Author              
Panjikar, Santosh3, Author
Fritzsch, Günter2, Author              
Stöckigt, Joachim1, Author
Affiliations:
1Department of Pharmaceutical Biology, Institute of Pharmacy, Johannes Gutenberg-University Mainz, 55099 Mainz, Germany., ou_persistent22              
2Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
3European Molecular Biology Laboratory, Hamburg Outstation, Deutsches Elektronen-Synchrotron, 22603 Hamburg, Germany, ou_persistent22              

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 Abstract: Vinorine synthase is an acetyltransferase that occupies a central role in the biosynthesis of the antiarrhythmic monoterpenoid indole alkaloid ajmaline in the plant Rauvolfia. Vinorine synthase belongs to the benzylalcohol acetyl-, anthocyanin-O-hydroxy-cinnamoyl-, anthranilate-N-hydroxy-cinnamoyl/benzoyl-, deacetylvindoline acetyltransferase (BAHD) enzyme superfamily, members of which are involved in the biosynthesis of several important drugs, such as morphine, Taxol, or vindoline, a precursor of the anti-cancer drugs vincaleucoblastine and vincristine. The x-ray structure of vinorine synthase is described at 2.6-Å resolution. Despite low sequence identity, the two-domain structure of vinorine synthase shows surprising similarity with structures of several CoA-dependent acyltransferases such as dihydrolipoyl transacetylase, polyketide-associated protein A5, and carnitine acetyltransferase. All conserved residues typical for the BAHD family are found in domain 1. His160 of the HXXXD motif functions as a general base during catalysis. It is located in the center of the reaction channel at the interface of both domains and is accessible from both sides. The channel runs through the entire molecule, allowing the substrate and co-substrate to bind independently. Asp164 points away from the catalytic site and seems to be of structural rather than catalytic importance. Surprisingly, the DFGWG motif, which is indispensable for the catalyzed reaction and unique to the BAHD family, is located far away from the active site and seems to play only a structural role. Vinorine synthase represents the first solved protein structure of the BAHD superfamily.

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Language(s): eng - English
 Dates: 2005-01-182004-12-232021-01-042005-04-08
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1074/jbc.M414508200
PMID: 15665331
 Degree: -

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Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 280 (14) Sequence Number: - Start / End Page: 13576 - 13583 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1