Related Experiment Video
Updated: May 13, 2025
10:19
Single-Molecule FRET Imaging for Observing the Conformational Dynamics of Dynamin-Like GTPase Atlastin
Published on: January 24, 2025
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Evolutionary insights into elongation factor G using AlphaFold and ancestral analysis.
Shawonur Rahaman1, Jacob H Steele2, Yi Zeng1
1Department of Chemistry, University of Houston, Houston, TX, 77204, USA.
Computers in Biology and Medicine
|April 13, 2025
Summary
Elongation factor G (EF-G) conformational flexibility shapes protein synthesis. AlphaFold and sequence analysis reveal EF-G
Area of Science:
- Molecular Biology
- Evolutionary Biology
- Structural Biology
Background:
- Elongation factor G (EF-G) is essential for ribosomal translocation during protein synthesis.
- The conformational dynamics and evolutionary history of EF-G are not fully understood.
Purpose of the Study:
- To investigate the conformational landscape and evolutionary divergence of EF-G.
- To understand how sequence variations influence EF-G conformation and function.
Main Methods:
- Integration of AlphaFold structural predictions with multiple sequence alignment (MSA)-based sequence analysis.
- Phylogenetic analysis and ancestral sequence reconstruction.
Main Results:
- Identified five high-confidence structural states of wild type EF-G, showing greater conformational diversity than previously known.
- Discovered that single-point mutations in the switch I loop affect the equilibrium between two main conformational states (con1 and con2).
- Reconstructed ancestral EF-Gs with reduced GTPase and translocase activity, indicating these functions evolved later.
Conclusions:
- Conformational flexibility is key to EF-G function and specialization.
- Robust translocase activity evolved after the divergence of major EF-G conformational states.
- The computational pipeline offers insights into the evolution of translational machinery.
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