2fp8: Difference between revisions

Revision as of 22:40, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2fp8.png

Template:STRUCTURE 2fp8

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

Template:ABSTRACT PUBMED 16531499

About this StructureAbout this Structure

2FP8 is a Single protein structure of sequence from Rauvolfia serpentina. 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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OCA

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-'''Structure of Strictosidine Synthase, the Biosynthetic Entry to the Monoterpenoid Indole Alkaloid Family'''
+===Structure of Strictosidine Synthase, the Biosynthetic Entry to the Monoterpenoid Indole Alkaloid Family===
-==Overview==
+<!--
-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 line below this paragraph, {{ABSTRACT_PUBMED_16531499}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_16531499}}
 ==About this Structure==
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 [[Category: Str1]]
 [[Category: Synthase]]
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