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Published on: October 25, 2017
Commensurability between protein nanotubes in contractile ejection nanomachines
Sergey B Rochal1, Daria S Roshal, Anna E Myasnikova
1Faculty of Physics, Southern Federal University, 5 Zorge str., 344090 Rostov-on-Don, Russia. rochal_s@yahoo.fr.
Contractile ejection nanomachines, like bacteriophage T4 tails, use sheath-tube assemblies for molecular transport. Their sheath contracts to match the inner tube, improving nanomachine efficiency and torque for cell membrane penetration.
Area of Science:
- Biophysics
- Structural Biology
- Nanotechnology
Background:
- Contractile ejection nanomachines, such as bacteriophage T4 tails and pyocin R2, are essential for translocating molecules across cell membranes.
- These machines function as sheath-tube assemblies, utilizing structural rearrangements for their operation.
Purpose of the Study:
- To investigate the geometrical relationship between the sheath and inner tube structures in contractile ejection nanomachines.
- To elucidate how sheath contraction and twisting impact nanomachine efficiency and function.
Main Methods:
- Analysis of the structural rearrangements in bacteriophage T4 tail and pyocin R2 sheath contraction.
- Application of the Frank and van der Merwe theory of commensurability to model protein nanotube interactions.
- Derivation of an expression for the interaction energy between the sheath and inner tube.
Main Results:
- The contracted sheath becomes commensurate with the inner tube, revealing a novel geometrical relationship between their symmetries.
- Commensurability between the sheath and inner tube reduces both interaction and total system energy.
- The observed energy gain enhances the torque of the inner tube, facilitating cell membrane penetration.
Conclusions:
- The commensurability of the contracted sheath with the inner tube is a key factor in the efficient operation of these nanomachines.
- This geometrical relationship optimizes energy transfer, leading to increased torque for membrane disruption.
- The findings provide fundamental insights into the mechanics of viral and bacterial protein nanomachines.
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