Changes in Dynamics upon Oligomerization Regulate Substrate Binding and Allostery in Amino Acid Kinase Family Members
2011
How Oligomerization Affects Protein Dynamics in Amino Acid Kinases
publication
Evidence: high
Author Information
Author(s): Marcos Enrique, Crehuet Ramon, Bahar Ivet
Primary Institution: Department of Biological Chemistry and Molecular Modelling, IQAC-CSIC, Barcelona, Spain
Hypothesis
The study investigates how oligomerization influences the dynamics and functional properties of amino acid kinases.
Conclusion
Oligomerization significantly alters the dynamics of amino acid kinases, affecting their substrate binding and allosteric regulation.
Supporting Evidence
- Oligomerization enhances the intrinsic dynamics of individual monomers.
- The study highlights the importance of interfacial interactions in protein function.
- Different oligomerization states lead to distinct collective motions.
- Cooperative inhibition mechanisms are elucidated for hexameric N-acetyl-L-glutamate kinase.
Takeaway
When proteins stick together to form larger groups, they can move differently, which helps them work better with other molecules.
Methodology
The study used an elastic network model to analyze the collective dynamics of enzymes in different oligomeric states.
Digital Object Identifier (DOI)
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