4IYG

Structure of strictosidine synthase in complex with 2-(1H-INDOL-3-YL)-N-METHYLETHANAMINE

Summary for 4IYG

• Entry DOI: 10.2210/pdb4iyg/pdb
• Descriptor: Strictosidine synthase, 2-(1H-indol-3-yl)-N-methylethanamine (3 entities in total)
• Functional Keywords: strictosidine synthase, lyase-lyase inhibitor complex, lyase/lyase inhibitor
• Biological source: Rauvolfia serpentina (devilpepper)
• Cellular location: Vacuole: P68175
• Total number of polymer chains: 2
• Total formula weight: 67561.45

Authors

Stoeckigt, J.,Fangrui, W.,Wang, M.,Rajendran, C. (deposition date: 2013-01-28, release date: 2014-01-29, Last modification date: 2024-11-06)

Primary citation

Zhu, H.,Kercmar, P.,Wu, F.,Rajendran, C.,Sun, L.,Wang, M.,Stockigt, J.
Using Strictosidine Synthase to Prepare Novel Alkaloids.
Curr.Med.Chem., 2015

PubMed Abstract: 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.

PubMed: 25850764

Experimental method

X-RAY DIFFRACTION (2.702 Å)