Related Experiment Video
Updated: Dec 19, 2025

Investigating Receptor-ligand Systems of the Cellulosome with AFM-based Single-molecule Force Spectroscopy
Published on: December 20, 2013
Deciphering effectual binding potential of xylo-substrates towards xylose isomerase and xylokinase through molecular
Sinosh Skariyachan1, Ishu Khangwal2, Vidya Niranjan3
1Department of Microbiology, St. Pius X College Rajapuram, Kasaragod, India.
Abstract:
Xylooligosaccharides (XOS) such as xylobiose and xylotriose are prebiotics with important functions and relevance and the study of interaction mechanism between these substrate and their respective enzymes has scope and applications. Thus, the present study aimed to decipher the interaction mechanisms of xylose isomerase (XylA) and xylokinase (XylB) towards their xylo-substrates namely xylobiose and xylotriose by computational modeling and molecular dynamic simulation studies. The three-dimensional structures of XylA and XylB, not available in their native forms, were predicted, energy minimized and validated by various computational biology tools and software. The binding mechanisms of xylobiose and xylotriose towards XylA and XylB were modeled by molecular docking and the stability of the docked complexes was confirmed by molecular dynamic (MD) simulation. The current study suggested that the theoretical models of XylA and XylB possessed good stereo-chemical validity, structural stabilities and minimum energy conformers. The molecular docking studied showed that xylotriose showed better binding interactions to XylA than xylobiose and xylobiose showed better binding interaction to XylB than xylotriose with ideal root mean square deviation (RMS), minimum binding energy (kcal/mol), hydrogen bonding and weak interactions. The MD simulation confirmed the stabilities of the docked complexes predicted by docking studies. The study suggested that interactions between the probiotics and prebiotics and provides the novel insights in exploring synbiotics as functional foods towards their futuristic applications. [Formula: see text]HighlightsThis study deciphers the interactions of xylosubstrates to XylA and XylB.The XylA and XylB possessed ideal structural stability and stereochemistryXylotriose and Xylobiose showed significant interactionsThe interactions of Xylotriose-XylA and Xylobiose-XylB were found stable in MD studies.Communicated by Ramaswamy H. Sarma.
More Related Videos
10:21Author Spotlight: Streamlining Protein Target Prediction and Validation via Molecular Docking and CETSA
Published on: February 23, 2024
08:49Incorporating Target Protein Structure Flexibility and Dynamics in Computational Drug Discovery Using Ensemble-Based Docking Analysis
Published on: June 20, 2025
Related Concept Videos
Ligand Binding and Linkage
The Equilibrium Binding Constant and Binding Strength
Ligand Binding Sites
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Induced-fit Model
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical...
Allosteric Proteins-ATCase
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...