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Plos One : Molecular Dynamics Reveal Binding Mode of Glutathionylspermidine by Trypanothione Synthetase, Volume 7

By Zilberstein, Dan

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Book Id: WPLBN0003957068
Format Type: PDF eBook :
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Reproduction Date: 2015

Title: Plos One : Molecular Dynamics Reveal Binding Mode of Glutathionylspermidine by Trypanothione Synthetase, Volume 7  
Author: Zilberstein, Dan
Volume: Volume 7
Language: English
Subject: Journals, Science, Medical Science
Collections: Periodicals: Journal and Magazine Collection
Historic
Publication Date:
Publisher: Plos

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Zilberstein, D. (n.d.). Plos One : Molecular Dynamics Reveal Binding Mode of Glutathionylspermidine by Trypanothione Synthetase, Volume 7. Retrieved from http://netlibrary.net/


Description
Description : The trypanothione synthetase (TryS) catalyses the two-step biosynthesis of trypanothione from spermidine and glutathione and is an attractive new drug target for the development of trypanocidal and antileishmanial drugs, especially since the structural information of TryS from Leishmania major has become available. Unfortunately, the TryS structure was solved without any of the substrates and lacks loop regions that are mechanistically important. This contribution describes docking and molecular dynamics simulations that led to further insights into trypanothione biosynthesis and, in particular, explains the binding modes of substrates for the second catalytic step. The structural model essentially confirm previously proposed binding sites for glutathione, ATP and two Mg2+ ions, which appear identical for both catalytic steps. The analysis of an unsolved loop region near the proposed spermidine binding site revealed a new pocket that was demonstrated to bind glutathionylspermidine in an inverted orientation. For the second step of trypanothione synthesis glutathionylspermidine is bound in a way that preferentially allows N1-glutathionylation of N8-glutathionylspermidine, classifying N8-glutathionylspermidine as the favoured substrate. By inhibitor docking, the binding site for N8-glutathionylspermidine was characterised as druggable.

 

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