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Structural flexibility of the periplasmic protein, FlgA, regulates flagellar P-ring assembly in Salmonella enterica.

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.

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Molecular Sculpture

by Eric Martz
A historical review on sculptures and physical models of macromolecules.

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Lifecycle of SARS-CoV-2

What happens if a SARS-CoV-2 coronavirus enters your lung? This molecular animation visualises how the virus particle can take over the host cell and turns it into a virus factory. Eventually, the host cell produces so many viral particles that it dies and releases numerous new virus particles. >>> Visit this page >>>