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Title

 

 

 

 

Insights of interaction between small and large subunits of ADP-glucose pyrophosphorylase from bread wheat (Triticum aestivum L.) 


Authors

Mohd Danishuddin, Ravish Chatrath, Rajender Singh*

 

Affiliation

Directorate of Wheat Research, Post Box 158, Karnal - 132001, India 


Email

rajenderkhokhar@yahoo.com; *Corresponding author

 

Article Type

Hypothesis

 

Date

Received July 26, 2010, Accepted January 29, 2011; Published May 07, 2011

 

Abstract

Lack of knowledge of three dimensional structures of small and large subunits of ADP- glucose pyrophosphorylase (AGPase) in wheat has hindered efforts to understand the binding specifities of substrate and catalytic mechanism. Thus, to understand the structure activity relationship, 3D structures were built by homology modelling based on crystal structure of potato tuber ADP-glucose pyrophosphorylase. Selected models were refined by energy minimization and further validated by Procheck and Prosa-web analysis. Ramachandran plot showed that overall main chain and side chain parameters are favourable. Moreover, Z-score of the models from Prosa-web analysis gave the conformation that they are in the range of the template. Interaction analysis depicts the involvement of six amino acids in hydrogen bonding (AGP-SThr422-AGP-LMet138, AGP- SArg420-AGP-LGly47, AGP-SSer259-AGP-LSer306, AGP-SGlu241-AGP-LIle311, AGP- SGln113-AGP-LGlu286 and AGP-SGln70-AGP-LLys291). Fifteen amino acids of small subunit were able to make hydrophobic contacts with seventeen amino acids of large subunit. Furthermore, decrease in the solvent accessible surface area in the amino acids involved in interaction were also reported. All the distances were formed in between 2.27 to 3.78. The present study focussed on heterodimeric structure of (AGPase). This predicted complex not only enhance our understanding of the interaction mechanism between these subunits (AGP-L and AGP-S) but also enable to further study to obtain better variants of this enzyme for the improvement of the plant yield.

 

Keywords

AGPase, ADP-glucose pyrophosphorylase, AGP-S, AGP-L, modelling, molecular docking, hydrogen bonding, hydrophobic contacts, accessible surface area.

 

Citation

Danishuddin et al. Bioinformation 6(4): 144-148 (2011)

 

Edited by

N Pattabiraman

 

ISSN

0973-2063

 

Publisher

Biomedical Informatics

 

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.