2fpc
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Structure of Strictosidine Synthase, the Biosynthetic Entry to the Monoterpenoid Indole Alkaloid Family
OverviewOverview
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.
About this StructureAbout this Structure
2FPC is a Single protein structure of sequence from Rauvolfia serpentina with SCG as ligand. Active as Strictosidine synthase, with EC number 4.3.3.2 Full crystallographic information is available from OCA.
ReferenceReference
The structure of Rauvolfia serpentina strictosidine synthase is a novel six-bladed beta-propeller fold in plant proteins., Ma X, Panjikar S, Koepke J, Loris E, Stockigt J, Plant Cell. 2006 Apr;18(4):907-20. Epub 2006 Mar 10. PMID:16531499
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