The protein “MIPS” changes its shape when it becomes active. Its center, which is usually disordered, forms a specific structure to perform essential functions. This protein helps produce inositol, or vitamin B8, which plays a critical role in the body.
Researchers from Martin Luther University Halle-Wittenberg have observed this process for the first time and found it may happen in similar proteins. Understanding how proteins change their structure is important because even small changes can affect their function and cause diseases.
The team studied the fungus Thermochaetoides thermophila to learn about a protein called MIPS, which helps produce inositol (vitamin B8). Even though inositol is essential, it’s not a proper vitamin because the body makes it.
Using cryo-electron microscopy, they found that MIPS exists in three states: disordered, ordered, and intermediate. They aren’t sure why the third state exists, but it may help with water absorption or other reactions. The researchers also found that over 340 similar proteins showed the same behavior.
The findings are helpful for more than just basic research. “Greater knowledge of metabolic pathways and the proteins involved may open new therapeutic approaches. Our work provides an important first step,” said Professor Panagiotis Kastritis, a biochemist at MLU.Â
Journal reference:
- Toni K. Träger, Fotis L. Kyrilis et al., Disorder-to-order active site capping regulates the rate-limiting step of the inositol pathway. PNAS. DOI: 10.1073/pnas.2400912121.
