This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: 18/4/907    most recent tpc.105.038018v1 Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Web of Science (17) Citing Articles via Google Scholar Google Scholar Articles by Ma, X. Articles by Stöckigt, J. Search for Related Content PubMed PubMed Citation Articles by Ma, X. Articles by Stöckigt, J. Agricola Articles by Ma, X. Articles by Stöckigt, J.

The Structure of Rauvolfia serpentina Strictosidine Synthase Is a Novel Six-Bladed ß-Propeller Fold in Plant Proteins^[W]

^a Department of Pharmaceutical Biology, Institute of Pharmacy, Johannes Gutenberg-University, D-55099 Mainz, Germany
^b European Molecular Biology Laboratory Hamburg Outstation DESY, D-22603 Hamburg, Germany
^c Department of Molecular Membrane Biology, Max-Planck-Institute of Biophysics, 60438 Frankfurt, Germany
^d College of Pharmaceutical Sciences, Zhejiang University, Hangzhou 310031, China

² To whom correspondence should be addressed. E-mail stoeckig{at}mail.uni-mainz.de; fax 49-6131-39-23752.

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 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 ß-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 ß-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.

This article has been cited by other articles:

				A. Ilari, S. Franceschini, A. Bonamore, F. Arenghi, B. Botta, A. Macone, A. Pasquo, L. Bellucci, and A. Boffi Structural Basis of Enzymatic (S)-Norcoclaurine Biosynthesis J. Biol. Chem., January 9, 2009; 284(2): 897 - 904. [Abstract] [Full Text] [PDF]

				L. Barleben, S. Panjikar, M. Ruppert, J. Koepke, and J. Stockigt Molecular Architecture of Strictosidine Glucosidase: The Gateway to the Biosynthesis of the Monoterpenoid Indole Alkaloid Family PLANT CELL, September 1, 2007; 19(9): 2886 - 2897. [Abstract] [Full Text] [PDF]