Sandbox Home

ST Huber, D Terwiel, WH Evers, D Maresca, AJ Jakobi. Preprint 2022 doi: 10.1101/2022.05.08.489936
Many kinds of bacteria and archaea control their buoyancy to move to optimal positions in liquid environments. They do this by making nano-compartments called "gas vesicles", long "pipes" with closed ends filled with gases. In 2022, gas vesicle structure was solved, revealing self-assembling thin-walled cylinders of remarkable strength with gas-permeable pores and water-repelling (hydrophobic) interiors. Building on this structural knowledge, gas vesicles are being engineered to serve as biosensors that report via ultrasound.

>>> Visit I3DC Interactive Visualizations >>>

H Matsunami, YH Yoon, VA Meshcheryakov, K Namba, FA Samatey. Scientific Reports 2016 doi: 10.1038/srep27399
A periplasmic flagellar chaperone protein, FlgA, is required for P-ring assembly in bacterial flagella of taxa such as Salmonella enterica or Escherichia coli. Here we present the open and closed crystal structures of FlgA from Salmonella enterica serovar Typhimurium, grown under different crystallization conditions. An intramolecular disulfide cross-linked form of FlgA caused a dominant negative effect on motility of the wild-type strain.

>>> Visit this I3DC complement >>>

Above is a transmembrane protein that takes up, into your intestinal cells, orally consumed peptide nutrients and drugs. Its lumen-face (shown above) opens and binds peptide or drug, then closes, while its cytoplasmic face (opposite end from the above) opens to release its cargo into the intestinal cell, which passes it on into the blood circulation.

>>> See more animations and explanation >>>