7RTX
Actophorin grown in microgravity
Summary for 7RTX
| Entry DOI | 10.2210/pdb7rtx/pdb |
| Descriptor | Actophorin (2 entities in total) |
| Functional Keywords | microgravity, motor protein |
| Biological source | Acanthamoeba castellanii (Amoeba) |
| Total number of polymer chains | 1 |
| Total formula weight | 15444.39 |
| Authors | Lieberman, R.L.,Quirk, S. (deposition date: 2021-08-16, release date: 2021-12-22, Last modification date: 2023-10-18) |
| Primary citation | Quirk, S.,Lieberman, R.L. Improved resolution crystal structure of Acanthamoeba actophorin reveals structural plasticity not induced by microgravity. Acta Crystallogr.,Sect.F, 77:452-458, 2021 Cited by PubMed Abstract: Actophorin, a protein that severs actin filaments isolated from the amoeba Acanthamoeba castellanii, was employed as a test case for crystallization under microgravity. Crystals of purified actophorin were grown under microgravity conditions aboard the International Space Station (ISS) utilizing an interactive crystallization setup between the ISS crew and ground-based experimenters. Crystals grew in conditions similar to those grown on earth. The structure was solved by molecular replacement at a resolution of 1.65 Å. Surprisingly, the structure reveals conformational changes in a remote β-turn region that were previously associated with actophorin phosphorylated at the terminal residue Ser1. Although crystallization under microgravity did not yield a higher resolution than crystals grown under typical laboratory conditions, the conformation of actophorin obtained from solving the structure suggests greater flexibility in the actophorin β-turn than previously appreciated and may be beneficial for the binding of actophorin to actin filaments. PubMed: 34866600DOI: 10.1107/S2053230X21011419 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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