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The structural basis of ATP as an allosteric modulator
Shaoyong Lu1, Wenkang Huang1, Qi Wang1
1Department of Pathophysiology, Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education, Shanghai JiaoTong University, School of Medicine, Shanghai, China.
Plos Computational Biology
|September 12, 2014
Summary
Adenosine-5'-triphosphate (ATP) exhibits distinct conformations influencing its biological roles. Understanding ATP
Area of Science:
- Biochemistry
- Molecular Biology
- Structural Biology
Background:
- Adenosine-5 '-triphosphate (ATP) is primarily known as an energy currency and for protein modification.
- Emerging research highlights ATP's allosteric role in cellular signal transduction, yet this function remains poorly understood.
Purpose of the Study:
- To investigate the conformational dynamics of ATP in solution and protein binding sites.
- To elucidate the mechanisms underlying ATP's allosteric regulation in biological systems.
Main Methods:
- Analysis of ATP in solution and protein complexes.
- Nudged elastic band simulations of ATP binding to uridine monophosphate kinase.
- Characterization of ATP conformations in substrate and allosteric binding sites.
Main Results:
- Free ATP exists in both compact and extended conformations in solution.
- ATP adopts different conformations in allosteric versus substrate binding sites.
- ATP preferentially binds to substrate sites in solution, with allosteric binding involving the triphosphate moiety.
Conclusions:
- ATP's distinct conformations are crucial for its diverse biological functions.
- The triphosphate and adenine parts of ATP contribute to allosteric signaling.
- This study provides a comprehensive understanding of ATP's allosteric regulatory mechanisms.
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