4IYG: Structure Of Strictosidine Synthase In Complex With 2-(1h-indol-3-yl)- N-methylethanamine

The Pictet-Spenglerasestrictosidine synthase (STR) has been characterized as the central enzyme in the biosynthesis of around 2000 monoterpenoid indole alkaloids in plants. In the light of a high therapeutic value and huge scaffold diversity these alkaloids represent, STR as an enzyme has attracted great attentions in recent years, intending to be utilized in the formation of new interesting alkaloids with unusual substitution pattern or even with novel scaffolds. For outlining the application potential that STR possesses, together with insight into the reaction mechanism catalyzed by STR, strategies and methods for exploring the applicability of STR have been updated in this article by taking R. serpertina STR(RS-STR) and C. roseus.STR (CR-STR) as representative models, followed by introducing the latest released complex structures of RS-STR with new substrates. Examples provided here, including substrate scaffold tailoring, X-ray crystal complex structure comparison, protein engineering and biosynthetic pathway reprogramming, pave the way to finally construct novel alkaloids libraries by chemo-enzymatic approaches.
PDB ID: 4IYGDownload
MMDB ID: 117009
PDB Deposition Date: 2013/1/28
Updated in MMDB: 2015/12
Experimental Method:
x-ray diffraction
Resolution: 2.7  Å
Source Organism:
Similar Structures:
Biological Unit for 4IYG: monomeric; determined by author and by software (PISA)
Molecular Components in 4IYG
Label Count Molecule
Protein (1 molecule)
Strictosidine Synthase
Molecule annotation
Chemical (1 molecule)
* Click molecule labels to explore molecular sequence information.

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