Monomer, dimer, and steered simulations of actin homologs
- The actin family of cytoskeletal proteins is essential to the physiology of virtually all archaea, bacteria, and eukaryotes. While X-ray crystallography and electron microscopy have revealed structural homologies among actin-family proteins, these techniques cannot probe molecular-scale conformational dynamics. Here, we use long-time scale, all-atom molecular dynamic simulations to reveal conserved dynamical behaviors in four prokaryotic actin homologs: MreB, FtsA, ParM, and crenactin. Simulations used for this study provide molecular-scale insights into the nucleotide and polymerization dependencies of the structure of prokaryotic actins, suggesting mechanisms for how these structural features are linked to their diverse functions.
|Type of resource
|August 2015 - June 2017
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- User agrees that, where applicable, content will not be used to identify or to otherwise infringe the privacy or confidentiality rights of individuals. Content distributed via the Stanford Digital Repository may be subject to additional license and use restrictions applied by the depositor.
- This work is licensed under a Creative Commons Attribution Non Commercial 3.0 Unported license (CC BY-NC).
- Preferred Citation
- Kerwyn Huang, Natalie Ng, Handuo Shi, and Alexandre Colavin. (2017). Monomer, dimer, and steered simulations of actin homologs. Stanford Digital Repository. Available at: https://purl.stanford.edu/cm430hn3276
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