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  The Structure of Rauvolfia serpentina Strictosidine Synthase Is a Novel Six-Bladed β-Propeller Fold in Plant Proteins

Ma, X., Panjikar, S., Koepke, J., Loris, E., & Stöckigt, J. (2006). The Structure of Rauvolfia serpentina Strictosidine Synthase Is a Novel Six-Bladed β-Propeller Fold in Plant Proteins. The Plant Cell, 18(4), 907-920. doi:10.1105/tpc.105.038018 Free PMC article.

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 Creators:
Ma, Xueyan1, Author
Panjikar, Santosh2, Author
Koepke, Jürgen3, Author              
Loris, Elke1, Author
Stöckigt, Joachim1, 4, Author
Affiliations:
1Department of Pharmaceutical Biology, Institute of Pharmacy, Johanes Gutenberg-University, 55099 Mainz, Germany., ou_persistent22              
2European Molecular Biology Laboratory Hamburg Outstation DESY, D-22603 Hamburg, Germany, ou_persistent22              
3Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
4College of Pharmaceutical Sciences, Zhejiang University, Hangzhou 310031, China, ou_persistent22              

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 Abstract: The enzyme strictosidine synthase (STR1) from the Indian medicinal plant Rauvolfia serpentina is of primary importance for the biosynthetic pathway of the indole alkaloid ajmaline. Moreover, STR1 initiates all biosynthetic pathways leading to the entire monoterpenoid indole alkaloid family representing an enormous structural variety of approximately 2000 compounds in higher plants. The crystal structures of STR1 in complex with its natural substrates tryptamine and secologanin provide structural understanding of the observed substrate preference and identify residues lining the active site surface that contact the substrates. STR1 catalyzes a Pictet-Spengler-type reaction and represents a novel six-bladed beta-propeller fold in plant proteins. Structure-based sequence alignment revealed a common repetitive sequence motif (three hydrophobic residues are followed by a small residue and a hydrophilic residue), indicating a possible evolutionary relationship between STR1 and several sequence-unrelated six-bladed beta-propeller structures. Structural analysis and site-directed mutagenesis experiments demonstrate the essential role of Glu-309 in catalysis. The data will aid in deciphering the details of the reaction mechanism of STR1 as well as other members of this enzyme family.

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Language(s): eng - English
 Dates: 2005-12-252005-09-162006-02-062006-03-102006-04-01
 Publication Status: Published in print
 Pages: 14
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: The Plant Cell
  Abbreviation : Plant C
Source Genre: Journal
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Publ. Info: Rockville : American Society of Plant Physiologists
Pages: - Volume / Issue: 18 (4) Sequence Number: - Start / End Page: 907 - 920 Identifier: ISSN: 1532-298X
CoNE: https://pure.mpg.de/cone/journals/resource/1532-298X