2fpb | pdb_00002fpb

Structure of Strictosidine Synthase, the Biosynthetic Entry to the Monoterpenoid Indole Alkaloid Family

spinqualitylabelsall models 2fpb, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2fpb is a 2 chain structure with sequence from Ophioxylon serpentinum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: TSS NonStd Res: MSE Activity: Strictosidine synthase, with EC number 4.3.3.2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [STSY_RAUSE] Catalyzes the stereospecific condensation of tryptamine with secologanin to form strictosidine, the key intermediate of indole alkaloid biosynthesis. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Strictosidine Synthase

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